{"title":"Transmembrane Proteins","description":"","products":[{"product_id":"recombinant-human-5-hydroxytryptamine-receptor-3d-htr3d-partial-bhp10503924","title":"Recombinant Human 5-hydroxytryptamine receptor 3D (HTR3D), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHTR3D\u003c\/strong\u003e (also reported as Serotonin receptor 3D) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eThis is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e HTR3D (also reported as Serotonin receptor 3D). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 221-454aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 41.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHTR3D has been annotated as This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: HTR3D — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HTR3D\n- NCBI Gene search: HTR3D — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HTR3D\n- Ensembl search: HTR3D — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HTR3D\n- AlphaFold DB search: HTR3D — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HTR3D\n- RCSB PDB search: HTR3D — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HTR3D\n- PubMed search: HTR3D transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HTR3D+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207321739629,"sku":"CSB-CF747864HU-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588657005,"sku":"CSB-CF747864HU-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF747864HU-SDS.jpg?v=1778623117"},{"product_id":"recombinant-human-c-x-c-chemokine-receptor-type-4-cxcr4-bhp10503916","title":"Recombinant Human C-X-C chemokine receptor type 4 (CXCR4)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCXCR4\u003c\/strong\u003e (also reported as FB22 Fusin HM89 LCR1 Leukocyte-derived seven transmembrane domain receptor Short name: LESTR Lipopolysaccharide-associated protein 3 Short name: LAP-3 Short name: LPS-associated protein 3 NPYRL Stromal cell-derived factor 1 receptor Short name: SDF-1 receptor CD_antigen: CD184) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for the C-X-C chemokine CXCL12\/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1\/MAPK3 activation.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CXCR4 (also reported as FB22 Fusin HM89 LCR1 Leukocyte-derived seven transmembrane domain receptor Short name: LESTR Lipopolysaccharide-associated protein 3 Short name: LAP-3 Short name: LPS-associated protein 3 NPYRL Stromal cell-derived factor 1 receptor Short name: SDF-1 receptor CD_antigen: CD184). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-356aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 56.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCXCR4 has been annotated as Receptor for the C-X-C chemokine CXCL12\/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1\/MAPK3 activation. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and\/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CXCR4 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CXCR4\n- NCBI Gene search: CXCR4 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CXCR4\n- Ensembl search: CXCR4 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CXCR4\n- AlphaFold DB search: CXCR4 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CXCR4\n- RCSB PDB search: CXCR4 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CXCR4\n- PubMed search: CXCR4 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CXCR4+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207321772397,"sku":"CSB-CF006254HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588591469,"sku":"CSB-CF006254HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF006254HU-SDS.jpg?v=1778623123"},{"product_id":"recombinant-human-c-x-c-chemokine-receptor-type-4-cxcr4-bhp10505928","title":"Recombinant Human C-X-C chemokine receptor type 4 (CXCR4)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCXCR4\u003c\/strong\u003e (also reported as FB22 Fusin HM89 LCR1 Leukocyte-derived seven transmembrane domain receptor) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for the C-X-C chemokine CXCL12\/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1\/MAPK3 activation.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CXCR4 (also reported as FB22 Fusin HM89 LCR1 Leukocyte-derived seven transmembrane domain receptor). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-356aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 44.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCXCR4 has been annotated as Receptor for the C-X-C chemokine CXCL12\/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1\/MAPK3 activation. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and\/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CXCR4 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CXCR4\n- NCBI Gene search: CXCR4 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CXCR4\n- Ensembl search: CXCR4 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CXCR4\n- AlphaFold DB search: CXCR4 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CXCR4\n- RCSB PDB search: CXCR4 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CXCR4\n- PubMed search: CXCR4 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CXCR4+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207321805165,"sku":"CSB-CF006254HUa0-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590983533,"sku":"CSB-CF006254HUa0-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF006254HUa0-SDS.jpg?v=1778623123"},{"product_id":"recombinant-vaccinia-virus-protein-i5-vacwr074-bhp10503912","title":"Recombinant Vaccinia virus Protein I5 (VACWR074)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eVACWR074\u003c\/strong\u003e (also reported as Protein VP13K) from Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)). In the supplied product notes, the target is described as \u003cem\u003eEnvelope protein\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e VACWR074 (also reported as Protein VP13K). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 2-79aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 24.6 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eVACWR074 has been annotated as Envelope protein.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: VACWR074 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=VACWR074\n- NCBI Gene search: VACWR074 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=VACWR074\n- Ensembl search: VACWR074 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=VACWR074\n- AlphaFold DB search: VACWR074 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/VACWR074\n- RCSB PDB search: VACWR074 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=VACWR074\n- PubMed search: VACWR074 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=VACWR074+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207321969005,"sku":"CSB-CF318298VAI-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588427629,"sku":"CSB-CF318298VAI-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF318298VAI-SDS.jpg?v=1778623123"},{"product_id":"recombinant-human-endothelin-1-receptor-ednra-bhp10503921","title":"Recombinant Human Endothelin-1 receptor (EDNRA)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eEDNRA\u003c\/strong\u003e (also reported as Endothelin A receptor) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for endothelin-1.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e EDNRA (also reported as Endothelin A receptor). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 21-427aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 48.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eEDNRA has been annotated as Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: EDNRA — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=EDNRA\n- NCBI Gene search: EDNRA — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=EDNRA\n- Ensembl search: EDNRA — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=EDNRA\n- AlphaFold DB search: EDNRA — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/EDNRA\n- RCSB PDB search: EDNRA — RCSB PDB — https:\/\/www.rcsb.org\/search?query=EDNRA\n- PubMed search: EDNRA transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=EDNRA+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322001773,"sku":"CSB-CF007403HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590164333,"sku":"CSB-CF007403HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF007403HU-SDS.jpg?v=1778623120"},{"product_id":"recombinant-human-claudin-6-cldn6-partial-bhp10503922","title":"Recombinant Human Claudin-6 (CLDN6), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN6\u003c\/strong\u003e (also reported as Skullin) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003ePlays a major role in tight junction-specific obliteration of the intercellular space (By similarity).\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CLDN6 (also reported as Skullin). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-82aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 24.8 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN6 has been annotated as Plays a major role in tight junction-specific obliteration of the intercellular space.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CLDN6 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN6\n- NCBI Gene search: CLDN6 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN6\n- Ensembl search: CLDN6 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN6\n- AlphaFold DB search: CLDN6 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN6\n- RCSB PDB search: CLDN6 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN6\n- PubMed search: CLDN6 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN6+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322034541,"sku":"CSB-CF005508HU-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320589050221,"sku":"CSB-CF005508HU-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF005508HU-SDS.jpg?v=1778623123"},{"product_id":"recombinant-influenza-a-virus-matrix-protein-2-m-bhp10503919","title":"Recombinant Influenza A virus Matrix protein 2 (M)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eM\u003c\/strong\u003e (also reported as M; M2; Matrix protein 2; Proton channel protein M2) from Influenza A virus (strain A\/USA:Phila\/1935 H1N1). In the supplied product notes, the target is described as \u003cem\u003eForms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e M (also reported as M; M2; Matrix protein 2; Proton channel protein M2). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-97aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 15.1 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eM has been annotated as Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: M — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=M\n- NCBI Gene search: M — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=M\n- Ensembl search: M — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=M\n- AlphaFold DB search: M — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/M\n- RCSB PDB search: M — RCSB PDB — https:\/\/www.rcsb.org\/search?query=M\n- PubMed search: M transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=M+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322067309,"sku":"CSB-CF389902ILU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591671661,"sku":"CSB-CF389902ILU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF389902ILU-SDS.jpg?v=1778623121"},{"product_id":"recombinant-oryza-sativa-subsp-japonica-os03g0263600-protein-os03g0263600-bhp10505913","title":"Recombinant Oryza sativa subsp. japonica Os03g0263600 protein (Os03g0263600)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Oryza sativa subsp. japonica (Rice): Oryza sativa subsp. japonica Os03g0263600 protein (Os03g0263600) corresponding to amino acids 1–427. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–427 (427 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 1TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Oryza sativa subsp. japonica (Rice). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q84Q89. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eOryza sativa subsp. japonica Os03g0263600 protein (Os03g0263600) is a membrane-associated protein from Oryza sativa subsp. japonica. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Oryza sativa subsp. japonica Os03g0263600 protein (Os03g0263600) (Q84Q89) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q84Q89\/entry\n- NCBI Gene search: Os03g0263600 Oryza sativa subsp. japonica — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Os03g0263600%20Oryza%20sativa%20subsp.%20japonica\n- PubMed search: Os03g0263600 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Os03g0263600%20review\n- InterPro search: Os03g0263600 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/Os03g0263600\/\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322100077,"sku":"CSB-CF2229OFG-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592097645,"sku":"CSB-CF2229OFG-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF2229OFG-SDS.jpg?v=1778623121"},{"product_id":"recombinant-human-5-hydroxytryptamine-receptor-1f-htr1f-bhp10505931","title":"Recombinant Human 5-hydroxytryptamine receptor 1F (HTR1F)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHTR1F\u003c\/strong\u003e (also reported as Serotonin receptor 1F) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eG-protein coupled receptor for 5-hydroxytryptamine (serotonin).\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e HTR1F (also reported as Serotonin receptor 1F). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-366aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 60.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHTR1F has been annotated as G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: HTR1F — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HTR1F\n- NCBI Gene search: HTR1F — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HTR1F\n- Ensembl search: HTR1F — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HTR1F\n- AlphaFold DB search: HTR1F — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HTR1F\n- RCSB PDB search: HTR1F — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HTR1F\n- PubMed search: HTR1F transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HTR1F+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322132845,"sku":"CSB-CF010886HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591245677,"sku":"CSB-CF010886HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF010886HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-potassium-channel-subfamily-k-member-3-kcnk3-bhp10506000","title":"Recombinant Human Potassium channel subfamily K member 3 (KCNK3)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eKCNK3\u003c\/strong\u003e (also reported as Acid-sensitive potassium channel protein TASK-1 (TWIK-related acid-sensitive K(+) channel 1) (Two pore potassium channel KT3.1) (Two pore K(+) channel KT3.1) (TASK) (TASK1)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003epH-dependent, voltage-insensitive, background potassium channel protein.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e KCNK3 (also reported as Acid-sensitive potassium channel protein TASK-1 (TWIK-related acid-sensitive K(+) channel 1) (Two pore potassium channel KT3.1) (Two pore K(+) channel KT3.1) (TASK) (TASK1)). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-394aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 50.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eKCNK3 has been annotated as pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: KCNK3 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=KCNK3\n- NCBI Gene search: KCNK3 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=KCNK3\n- Ensembl search: KCNK3 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=KCNK3\n- AlphaFold DB search: KCNK3 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/KCNK3\n- RCSB PDB search: KCNK3 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=KCNK3\n- PubMed search: KCNK3 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=KCNK3+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322165613,"sku":"CSB-CF012071HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590917997,"sku":"CSB-CF012071HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF012071HU-SDS.jpg?v=1778623123"},{"product_id":"recombinant-human-arachidonate-5-lipoxygenase-activating-protein-alox5ap-bhp10505942","title":"Recombinant Human Arachidonate 5-lipoxygenase-activating protein (ALOX5AP)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eALOX5AP\u003c\/strong\u003e (also reported as FLAP MK-886-binding protein) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eRequired for leukotriene biosynthesis by ALOX5 (5-lipoxygenase).\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e ALOX5AP (also reported as FLAP MK-886-binding protein). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-161aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 34.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eALOX5AP has been annotated as Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: ALOX5AP — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ALOX5AP\n- NCBI Gene search: ALOX5AP — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ALOX5AP\n- Ensembl search: ALOX5AP — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ALOX5AP\n- AlphaFold DB search: ALOX5AP — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ALOX5AP\n- RCSB PDB search: ALOX5AP — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ALOX5AP\n- PubMed search: ALOX5AP transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ALOX5AP+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322198381,"sku":"CSB-CF001625HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592851309,"sku":"CSB-CF001625HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF001625HU-SDS.jpg?v=1778623120"},{"product_id":"recombinant-yersinia-enterocolitica-protein-yopb-yopb-bhp10503911","title":"Recombinant Yersinia enterocolitica Protein YopB (yopB)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Yersinia enterocolitica: Yersinia enterocolitica Protein YopB (yopB) corresponding to amino acids 1–401. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–401 (401 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 2TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Yersinia enterocolitica. Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P37131. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eYersinia enterocolitica Protein YopB (yopB) is derived from Yersinia enterocolitica and is associated with bacterial virulence. YopB-family proteins are components of the type III secretion system (T3SS) translocon in several Yersinia species, where they help form pores that deliver effector proteins into host cells. Functional notes for this entry state it plays a role in virulence. Virulence factors are frequently studied for their interactions with host membranes and immune responses, and defined recombinant regions can support mechanistic and immunological studies. Also reported as: yopB; Protein YopB.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eHost–pathogen interaction research mapping T3SS assembly and translocon pore formation at host membranes.\u003c\/li\u003e\n\u003cli\u003eIdentification of neutralizing antibodies or inhibitors that disrupt translocation (RUO).\u003c\/li\u003e\n\u003cli\u003eComparative analyses of virulence factor variation across strains and its impact on host range and immune evasion.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eUse as a defined antigen for antibody generation or serology-oriented research assays (RUO).\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies with host membrane components or partner T3SS proteins.\u003c\/li\u003e\n\u003cli\u003eComparative studies of YopB-like proteins across Yersinia and related pathogens.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Yersinia enterocolitica Protein YopB (yopB) (P37131) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P37131\/entry\n- NCBI Gene search: yopB Yersinia enterocolitica — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=yopB%20Yersinia%20enterocolitica\n- PubMed search: yopB review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=yopB%20review\n- InterPro search: yopB — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/yopB\/\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322231149,"sku":"CSB-CF334228YAQ-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588329325,"sku":"CSB-CF334228YAQ-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF334228YAQ-SDS.jpg?v=1778623120"},{"product_id":"recombinant-human-5-hydroxytryptamine-receptor-2b-htr2b-bhp10503917","title":"Recombinant Human 5-hydroxytryptamine receptor 2B (HTR2B)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHTR2B\u003c\/strong\u003e (also reported as Serotonin receptor 2B) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eG-protein coupled receptor for 5-hydroxytryptamine (serotonin).\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e HTR2B (also reported as Serotonin receptor 2B). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-481aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 70.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHTR2B has been annotated as G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: HTR2B — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HTR2B\n- NCBI Gene search: HTR2B — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HTR2B\n- Ensembl search: HTR2B — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HTR2B\n- AlphaFold DB search: HTR2B — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HTR2B\n- RCSB PDB search: HTR2B — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HTR2B\n- PubMed search: HTR2B transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HTR2B+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322263917,"sku":"CSB-CF010888HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588951917,"sku":"CSB-CF010888HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF010888HU-SDS.jpg?v=1778623119"},{"product_id":"recombinant-human-transmembrane-protein-65-tmem65-partial-bhp10503927","title":"Recombinant Human Transmembrane protein 65 (TMEM65), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eTMEM65\u003c\/strong\u003e (also reported as TMEM65; TMM65_HUMAN; Transmembrane protein 65) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003ePlays an important role in cardiac development and function.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e TMEM65 (also reported as TMEM65; TMM65_HUMAN; Transmembrane protein 65). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 63-240aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 35.1 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eTMEM65 has been annotated as May play an important role in cardiac development and function. May regulate cardiac conduction and the function of the gap junction protein GJA1. May contributes to the stability and proper localization of GJA1 to cardiac intercalated disk thereby regulating gap junction communication (By similarity). May also play a role in the regulation of mitochondrial respiration and mitochondrial DNA copy number maintenance. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: TMEM65 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=TMEM65\n- NCBI Gene search: TMEM65 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=TMEM65\n- Ensembl search: TMEM65 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=TMEM65\n- AlphaFold DB search: TMEM65 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/TMEM65\n- RCSB PDB search: TMEM65 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=TMEM65\n- PubMed search: TMEM65 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=TMEM65+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322296685,"sku":"CSB-CF023869HU-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592523629,"sku":"CSB-CF023869HU-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF023869HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-lampetra-fluviatilis-nadh-ubiquinone-oxidoreductase-chain-1-mt-nd1-bhp10505943","title":"Recombinant Lampetra fluviatilis NADH-ubiquinone oxidoreductase chain 1 (MT-ND1)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMT-ND1\u003c\/strong\u003e (also reported as NADH dehydrogenase subunit 1 MTND1, NADH1, ND1) from Lampetra fluviatilis (European river lamprey) (Petromyzon fluviatilis). In the supplied product notes, the target is described as \u003cem\u003eCore subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e MT-ND1 (also reported as NADH dehydrogenase subunit 1 MTND1, NADH1, ND1). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-321aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 53.8 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eMT-ND1 has been annotated as Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: MT-ND1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=MT-ND1\n- NCBI Gene search: MT-ND1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MT-ND1\n- Ensembl search: MT-ND1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=MT-ND1\n- AlphaFold DB search: MT-ND1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/MT-ND1\n- RCSB PDB search: MT-ND1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=MT-ND1\n- PubMed search: MT-ND1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MT-ND1+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322329453,"sku":"CSB-CF015076LNM(A4)-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591737197,"sku":"CSB-CF015076LNM(A4)-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF015076LNM_A4_-SDS.jpg?v=1778623122"},{"product_id":"recombinant-mouse-high-affinity-immunoglobulin-epsilon-receptor-subunit-alpha-fcer1a-bhp10505908","title":"Recombinant Mouse High affinity immunoglobulin epsilon receptor subunit alpha (Fcer1a)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eFcer1a\u003c\/strong\u003e (also reported as Fc-epsilon RI-alpha) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003eBinds to the Fc region of immunoglobulins epsilon.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Fcer1a (also reported as Fc-epsilon RI-alpha). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 24-250aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 44.7 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eFcer1a has been annotated as Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Fcer1a — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Fcer1a\n- NCBI Gene search: Fcer1a — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Fcer1a\n- Ensembl search: Fcer1a — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Fcer1a\n- AlphaFold DB search: Fcer1a — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Fcer1a\n- RCSB PDB search: Fcer1a — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Fcer1a\n- PubMed search: Fcer1a transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Fcer1a+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322362221,"sku":"CSB-CF008532MO-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588394861,"sku":"CSB-CF008532MO-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF008532MO-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-atp-binding-cassette-sub-family-b-member-8-mitochondrial-abcb8-partial-bhp10503925","title":"Recombinant Human ATP-binding cassette sub-family B member 8, mitochondrial (ABCB8), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Homo sapiens (Human): Human ATP-binding cassette sub-family B member 8, mitochondrial (ABCB8), partial corresponding to amino acids 38–693. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 38–693 (656 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 3TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q9NUT2. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman ATP-binding cassette sub-family B member 8, mitochondrial (ABCB8), partial belongs to the ATP-binding cassette (ABC) transporter superfamily. ABC transporters use ATP binding and hydrolysis to power conformational changes that move substrates across membranes or regulate transport-related processes. In eukaryotes, mitochondrial ABC transporters are commonly studied in the context of organelle homeostasis, including metabolite transport and redox\/metal handling. For membrane transporters, the relationship between sequence, transmembrane architecture, and substrate specificity is a central theme. Also reported as: Mitochondrial ATP-binding cassette 1; ; M-ABC1.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eMechanistic transporter studies that link ATPase activity, conformational cycling, and substrate recognition (often integrating structural and biochemical data).\u003c\/li\u003e\n\u003cli\u003eDisease- and physiology-oriented research connecting ABC transporters to cellular homeostasis and stress responses (interpreted in model systems).\u003c\/li\u003e\n\u003cli\u003eDevelopment of inhibitors\/modulators and assays that probe transporter function, specificity, and regulation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody development or binder screening against defined regions of an ABC transporter.\u003c\/li\u003e\n\u003cli\u003eDomain-focused biochemical studies (e.g., interaction mapping with partner proteins or lipids) where the expressed region is critical for interpretation.\u003c\/li\u003e\n\u003cli\u003eComparative studies across orthologs or variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human ATP-binding cassette sub-family B member 8, mitochondrial (ABCB8), partial (Q9NUT2) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q9NUT2\/entry\n- NCBI Gene search: ABCB8 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ABCB8%20Homo%20sapiens\n- PubMed search: ABCB8 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ABCB8%20review\n- InterPro search: ABCB8 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/ABCB8\/\n- Ensembl Gene Summary: ABCB8 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=ABCB8\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322394989,"sku":"CSB-CF868325HU-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591311213,"sku":"CSB-CF868325HU-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF868325HU-SDS.jpg?v=1778623124"},{"product_id":"recombinant-mouse-calcium-uniporter-protein-mitochondrial-mcu-bhp10506891","title":"Recombinant Mouse Calcium uniporter protein, mitochondrial (Mcu)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMcu\u003c\/strong\u003e (also reported as Mcu; Calcium uniporter protein; mitochondrial) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003eMitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Mcu (also reported as Mcu; Calcium uniporter protein; mitochondrial). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 50-350aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 37.7 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eMcu is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Mcu — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Mcu\n- NCBI Gene search: Mcu — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Mcu\n- Ensembl search: Mcu — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Mcu\n- AlphaFold DB search: Mcu — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Mcu\n- RCSB PDB search: Mcu — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Mcu\n- PubMed search: Mcu transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Mcu+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322427757,"sku":"CSB-CF668882MO-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592884077,"sku":"CSB-CF668882MO-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF668882MO-1.jpg?v=1778623124"},{"product_id":"recombinant-human-blood-group-rh-d-polypeptide-rhd-bhp10505953","title":"Recombinant Human Blood group Rh (D) polypeptide (RHD)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eRHD\u003c\/strong\u003e (also reported as RHXIII Rh polypeptide 2 Short name: RhPII Rhesus D antigen CD_antigen: CD240D) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eMay be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e RHD (also reported as RHXIII Rh polypeptide 2 Short name: RhPII Rhesus D antigen CD_antigen: CD240D). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 2-417aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 47.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eRHD has been annotated as May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: RHD — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=RHD\n- NCBI Gene search: RHD — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=RHD\n- Ensembl search: RHD — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=RHD\n- AlphaFold DB search: RHD — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/RHD\n- RCSB PDB search: RHD — RCSB PDB — https:\/\/www.rcsb.org\/search?query=RHD\n- PubMed search: RHD transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=RHD+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322526061,"sku":"CSB-CF019677HU(A4)-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320593539437,"sku":"CSB-CF019677HU(A4)-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF019677HU_A4_-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-p53-apoptosis-effector-related-to-pmp-22-perp-bhp10505924","title":"Recombinant Human p53 apoptosis effector related to PMP-22 (PERP)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003ePERP\u003c\/strong\u003e (also reported as Keratinocyte-associated protein 1) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eComponent of intercellular desmosome junctions.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e PERP (also reported as Keratinocyte-associated protein 1). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-193aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 41.4 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ePERP has been annotated as Component of intercellular desmosome junctions. Plays a role in stratified epithelial integrity and cell-cell adhesion by promoting desmosome assembly. Plays a role as an effector in the TP53-dependent apoptotic pathway (By similarity).. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: PERP — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=PERP\n- NCBI Gene search: PERP — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=PERP\n- Ensembl search: PERP — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=PERP\n- AlphaFold DB search: PERP — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/PERP\n- RCSB PDB search: PERP — RCSB PDB — https:\/\/www.rcsb.org\/search?query=PERP\n- PubMed search: PERP transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=PERP+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322460525,"sku":"CSB-CF839325HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591606125,"sku":"CSB-CF839325HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF839325HU-SDS.jpg?v=1778623124"},{"product_id":"recombinant-rat-peripheral-myelin-protein-22-pmp22-bhp10505998","title":"Recombinant Rat Peripheral myelin protein 22 (Pmp22)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003ePmp22\u003c\/strong\u003e (also reported as Protein CD25 (SR13 myelin protein) (Schwann cell membrane glycoprotein) (SAG) (Cd25) (Pmp-22)) from Rattus norvegicus (Rat). In the supplied product notes, the target is described as \u003cem\u003eMight be involved in growth regulation, and in myelinization in the peripheral nervous system.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Pmp22 (also reported as Protein CD25 (SR13 myelin protein) (Schwann cell membrane glycoprotein) (SAG) (Cd25) (Pmp-22)). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-160aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 23.4 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ePmp22 has been annotated as Might be involved in growth regulation, and in myelinization in the peripheral nervous system.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Pmp22 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Pmp22\n- NCBI Gene search: Pmp22 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Pmp22\n- Ensembl search: Pmp22 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Pmp22\n- AlphaFold DB search: Pmp22 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Pmp22\n- RCSB PDB search: Pmp22 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Pmp22\n- PubMed search: Pmp22 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Pmp22+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322493293,"sku":"CSB-CF018241RA-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320593572205,"sku":"CSB-CF018241RA-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF018241RA-SDS.jpg?v=1778623123"},{"product_id":"recombinant-plasmodium-berghei-major-facilitator-superfamily-domain-containing-protein-partial-bhp10505910","title":"Recombinant Plasmodium berghei Major facilitator superfamily domain-containing protein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Plasmodium berghei: Plasmodium berghei Major facilitator superfamily domain-containing protein, partial (PBK173_000211300) corresponding to amino acids 756–960. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 756–960 (205 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 6TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Plasmodium berghei. Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt A0A0Y9WQZ1. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ePlasmodium berghei Major facilitator superfamily domain-containing protein, partial (PBK173_000211300) is annotated as a major facilitator superfamily (MFS) domain-containing protein. MFS proteins are ubiquitous secondary transporters that typically use electrochemical gradients to move small molecules across membranes. In parasites and microbes, MFS transporters are often investigated for roles in nutrient uptake, metabolite exchange, and drug susceptibility.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eTransporter annotation and substrate prediction using comparative genomics, conserved motif analysis, and structural modeling.\u003c\/li\u003e\n\u003cli\u003eStudies of transporter contributions to antimicrobial\/antiparasitic drug response and resistance mechanisms.\u003c\/li\u003e\n\u003cli\u003eReconstitution and binding-focused approaches to connect specific sequence regions to transport activity (interpretation-focused).\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eUse as a defined antigen for generating reagents that recognize MFS-family proteins or specific loops\/domains.\u003c\/li\u003e\n\u003cli\u003eBiochemical or biophysical characterization of an expressed region to support structure–function hypotheses.\u003c\/li\u003e\n\u003cli\u003eComparative expression studies across life-cycle stages or conditions to contextualize transporter regulation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Plasmodium berghei Major facilitator superfamily domain-containing protein, partial (PBK173_000211300) (A0A0Y9WQZ1) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/A0A0Y9WQZ1\/entry\n- NCBI Gene search: PBK173_000211300 Plasmodium berghei — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=PBK173_000211300%20Plasmodium%20berghei\n- PubMed search: PBK173_000211300 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=PBK173_000211300%20review\n- InterPro search: PBK173_000211300 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/PBK173_000211300\/\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322558829,"sku":"CSB-CF2221PLHa2-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590066029,"sku":"CSB-CF2221PLHa2-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF2221PLHa2-SDS.jpg?v=1778623121"},{"product_id":"recombinant-human-adiponectin-receptor-protein-1-adipor1-partial-bhp10507058","title":"Recombinant Human Adiponectin receptor protein 1 (ADIPOR1), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eADIPOR1\u003c\/strong\u003e (also reported as Progestin and adipoQ receptor family member 1 (Progestin and adipoQ receptor family member I) (PAQR1) (TESBP1A)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e ADIPOR1 (also reported as Progestin and adipoQ receptor family member 1 (Progestin and adipoQ receptor family member I) (PAQR1) (TESBP1A)). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 89-375aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 34.8 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eADIPOR1 is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: ADIPOR1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ADIPOR1\n- NCBI Gene search: ADIPOR1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ADIPOR1\n- Ensembl search: ADIPOR1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ADIPOR1\n- AlphaFold DB search: ADIPOR1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ADIPOR1\n- RCSB PDB search: ADIPOR1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ADIPOR1\n- PubMed search: ADIPOR1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ADIPOR1+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322657133,"sku":"CSB-CF001367HU2-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320593670509,"sku":"CSB-CF001367HU2-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF001367HU2-SDS.jpg?v=1778623118"},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-6-ccr6-bhp10505939","title":"Recombinant Human C-C chemokine receptor type 6 (CCR6)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCCR6\u003c\/strong\u003e (also reported as Chemokine receptor-like 3) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for the C-C type chemokine CCL20.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CCR6 (also reported as Chemokine receptor-like 3). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-374aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 46.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCCR6 has been annotated as Receptor for the C-C type chemokine CCL20. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CCR6 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CCR6\n- NCBI Gene search: CCR6 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR6\n- Ensembl search: CCR6 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CCR6\n- AlphaFold DB search: CCR6 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CCR6\n- RCSB PDB search: CCR6 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CCR6\n- PubMed search: CCR6 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR6+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322624365,"sku":"CSB-CF004845HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591081837,"sku":"CSB-CF004845HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF004845HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-acetolactate-synthase-like-protein-ilvbl-bhp10508840","title":"Recombinant Human Acetolactate synthase-like protein (ILVBL)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Homo sapiens (Human): Human Acetolactate synthase-like protein (ILVBL) corresponding to amino acids 1–632. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–632 (632 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 1TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt A1L0T0. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Acetolactate synthase-like protein (ILVBL) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: IlvB-like protein.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Acetolactate synthase-like protein (ILVBL) (A1L0T0) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/A1L0T0\/entry\n- NCBI Gene search: ILVBL Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ILVBL%20Homo%20sapiens\n- PubMed search: ILVBL review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ILVBL%20review\n- InterPro search: ILVBL — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/ILVBL\/\n- Ensembl Gene Summary: ILVBL (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=ILVBL\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322591597,"sku":"CSB-CF011687HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592130413,"sku":"CSB-CF011687HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF011687HU-SDS.jpg?v=1778623121"},{"product_id":"recombinant-sindbis-virus-structural-polyprotein-partial-bhp10505938","title":"Recombinant Sindbis virus Structural polyprotein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eRecombinant Sindbis virus Structural polyprotein, partial\u003c\/strong\u003e (also reported as p130) from Sindbis virus (SINV). In the supplied product notes, the target is described as \u003cem\u003eCapsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Recombinant Sindbis virus Structural polyprotein, partial (also reported as p130). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 807-1245aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 67.4 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eRecombinant Sindbis virus Structural polyprotein, partial has been annotated as Capsid protein. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Recombinant Sindbis virus Structural polyprotein, partial — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- NCBI Gene search: Recombinant Sindbis virus Structural polyprotein, partial — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- Ensembl search: Recombinant Sindbis virus Structural polyprotein, partial — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- AlphaFold DB search: Recombinant Sindbis virus Structural polyprotein, partial — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- RCSB PDB search: Recombinant Sindbis virus Structural polyprotein, partial — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- PubMed search: Recombinant Sindbis virus Structural polyprotein, partial transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322689901,"sku":"CSB-CF361018SHZ-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320589607277,"sku":"CSB-CF361018SHZ-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF361018SHZ-SDS.jpg?v=1778623122"},{"product_id":"recombinant-plasmodium-berghei-major-facilitator-superfamily-domain-containing-protein-partial-bhp10505909","title":"Recombinant Plasmodium berghei Major facilitator superfamily domain-containing protein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Plasmodium berghei: Plasmodium berghei Major facilitator superfamily domain-containing protein, partial (PBK173_000211300) corresponding to amino acids 756–960. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 756–960 (205 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 6TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Plasmodium berghei. Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt A0A0Y9WQZ1. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ePlasmodium berghei Major facilitator superfamily domain-containing protein, partial (PBK173_000211300) is annotated as a major facilitator superfamily (MFS) domain-containing protein. MFS proteins are ubiquitous secondary transporters that typically use electrochemical gradients to move small molecules across membranes. In parasites and microbes, MFS transporters are often investigated for roles in nutrient uptake, metabolite exchange, and drug susceptibility.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eTransporter annotation and substrate prediction using comparative genomics, conserved motif analysis, and structural modeling.\u003c\/li\u003e\n\u003cli\u003eStudies of transporter contributions to antimicrobial\/antiparasitic drug response and resistance mechanisms.\u003c\/li\u003e\n\u003cli\u003eReconstitution and binding-focused approaches to connect specific sequence regions to transport activity (interpretation-focused).\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eUse as a defined antigen for generating reagents that recognize MFS-family proteins or specific loops\/domains.\u003c\/li\u003e\n\u003cli\u003eBiochemical or biophysical characterization of an expressed region to support structure–function hypotheses.\u003c\/li\u003e\n\u003cli\u003eComparative expression studies across life-cycle stages or conditions to contextualize transporter regulation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Plasmodium berghei Major facilitator superfamily domain-containing protein, partial (PBK173_000211300) (A0A0Y9WQZ1) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/A0A0Y9WQZ1\/entry\n- NCBI Gene search: PBK173_000211300 Plasmodium berghei — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=PBK173_000211300%20Plasmodium%20berghei\n- PubMed search: PBK173_000211300 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=PBK173_000211300%20review\n- InterPro search: PBK173_000211300 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/PBK173_000211300\/\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322722669,"sku":"CSB-CF2221PLH-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588460397,"sku":"CSB-CF2221PLH-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF2221PLH-SDS.jpg?v=1778623121"},{"product_id":"recombinant-escherichia-coli-colicin-e1-cea-bhp10505954","title":"Recombinant Escherichia coli Colicin-E1 (cea)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003ecea\u003c\/strong\u003e (also reported as cea; Colicin-E1) from Escherichia coli. In the supplied product notes, the target is described as \u003cem\u003eThis colicin is a channel-forming colicin.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e cea (also reported as cea; Colicin-E1). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-522aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 64.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ecea has been annotated as This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; FUNCTION. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: cea — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=cea\n- NCBI Gene search: cea — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=cea\n- Ensembl search: cea — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=cea\n- AlphaFold DB search: cea — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/cea\n- RCSB PDB search: cea — RCSB PDB — https:\/\/www.rcsb.org\/search?query=cea\n- PubMed search: cea transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=cea+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322755437,"sku":"CSB-CF360926ENL-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588820845,"sku":"CSB-CF360926ENL-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF360926ENL-SDS.jpg?v=1778623121"},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-4-ccr4-active-bhp10505936","title":"Recombinant Human C-C chemokine receptor type 4 (CCR4) (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCCR4\u003c\/strong\u003e (also reported as C-C chemokine receptor type 4; C-C CKR-4; CC-CKR-4; CCR-4; CCR4; K5-5; CD194) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eHigh affinity receptor for the C-C type chemokines CCL17\/TARC, CCL22\/MDC and CKLF isoform 1\/CKLF1.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CCR4 (also reported as C-C chemokine receptor type 4; C-C CKR-4; CC-CKR-4; CCR-4; CCR4; K5-5; CD194). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-360aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 44.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCCR4 has been annotated as High affinity receptor for the C-C type chemokines CCL17\/TARC, CCL22\/MDC and CKLF isoform 1\/CKLF1. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Can function as a chemoattractant homing receptor on circulating memory lymphocytes and as a coreceptor for some primary HIV-2 isolates. In the CNS, could mediate hippocampal-neuron survival.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CCR4 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CCR4\n- NCBI Gene search: CCR4 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR4\n- Ensembl search: CCR4 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CCR4\n- AlphaFold DB search: CCR4 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CCR4\n- RCSB PDB search: CCR4 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CCR4\n- PubMed search: CCR4 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR4+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322788205,"sku":"CSB-CF004843HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320593113453,"sku":"CSB-CF004843HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF004843HU-SDS.jpg?v=1778623120"},{"product_id":"recombinant-human-atp-binding-cassette-sub-family-d-member-1-abcd1-active-bhp10506097","title":"Recombinant Human ATP-binding cassette sub-family D member 1 (ABCD1) (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eABCD1\u003c\/strong\u003e (also reported as Adrenoleukodystrophy protein) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eProbable transporter.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e ABCD1 (also reported as Adrenoleukodystrophy protein). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-745aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 84.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eABCD1 is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Transporters and pumps commonly control nutrient uptake, metabolite exchange, and ion gradients; isoform usage, substrate availability, and membrane microenvironment can all influence functional readouts.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: ABCD1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ABCD1\n- NCBI Gene search: ABCD1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ABCD1\n- Ensembl search: ABCD1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ABCD1\n- AlphaFold DB search: ABCD1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ABCD1\n- RCSB PDB search: ABCD1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ABCD1\n- PubMed search: ABCD1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ABCD1+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322820973,"sku":"CSB-CF001068HU-100UG","price":3500.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590688621,"sku":"CSB-CF001068HU-20UG","price":2160.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF001068HU-SDS.jpg?v=1778623125"},{"product_id":"recombinant-human-stearoyl-coa-desaturase-scd-bhp10505946","title":"Recombinant Human Stearoyl-CoA desaturase (SCD)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eSCD\u003c\/strong\u003e (also reported as Delta(9)-desaturase Short name: Delta-9 desaturase Fatty acid desaturase Stearoyl-CoA desaturase1 Short name: hSCD1) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eStearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e SCD (also reported as Delta(9)-desaturase Short name: Delta-9 desaturase Fatty acid desaturase Stearoyl-CoA desaturase1 Short name: hSCD1). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-359aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 44.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eSCD has been annotated as Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: SCD — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=SCD\n- NCBI Gene search: SCD — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=SCD\n- Ensembl search: SCD — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=SCD\n- AlphaFold DB search: SCD — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/SCD\n- RCSB PDB search: SCD — RCSB PDB — https:\/\/www.rcsb.org\/search?query=SCD\n- PubMed search: SCD transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SCD+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322853741,"sku":"CSB-CF020802HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592425325,"sku":"CSB-CF020802HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF020802HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-mouse-protein-dihydroorotate-dehydrogenase-quinone-mitochondrial-dhodh-bhp10505945","title":"Recombinant Mouse Protein Dihydroorotate dehydrogenase (quinone), mitochondrial(Dhodh)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eDhodh\u003c\/strong\u003e (also reported as Dihydroorotate oxidase) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003eCatalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Dhodh (also reported as Dihydroorotate oxidase). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 11-395aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 44.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eDhodh has been annotated as Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Dhodh — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Dhodh\n- NCBI Gene search: Dhodh — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Dhodh\n- Ensembl search: Dhodh — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Dhodh\n- AlphaFold DB search: Dhodh — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Dhodh\n- RCSB PDB search: Dhodh — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Dhodh\n- PubMed search: Dhodh transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Dhodh+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322886509,"sku":"CSB-CF006852MO-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320589345133,"sku":"CSB-CF006852MO-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF006852MO-SDS.jpg?v=1778623120"},{"product_id":"recombinant-human-5-hydroxytryptamine-receptor-3e-htr3e-partial-bhp10503926","title":"Recombinant Human 5-hydroxytryptamine receptor 3E (HTR3E), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHTR3E\u003c\/strong\u003e (also reported as Serotonin receptor 3E) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eThis is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e HTR3E (also reported as Serotonin receptor 3E). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 72-229aa\u0026amp;241-456aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 58.2 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHTR3E has been annotated as This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: HTR3E — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HTR3E\n- NCBI Gene search: HTR3E — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HTR3E\n- Ensembl search: HTR3E — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HTR3E\n- AlphaFold DB search: HTR3E — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HTR3E\n- RCSB PDB search: HTR3E — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HTR3E\n- PubMed search: HTR3E transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HTR3E+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322919277,"sku":"CSB-CF010894HU-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320589443437,"sku":"CSB-CF010894HU-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF010894HU-SDS.jpg?v=1778623121"},{"product_id":"recombinant-human-gamma-secretase-subunit-aph-1a-aph1a-bhp10503923","title":"Recombinant Human Gamma-secretase subunit APH-1A (APH1a)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eAPH1a\u003c\/strong\u003e (also reported as Aph-1alpha Presenilin-stabilization factor) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eEssential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein).\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e APH1a (also reported as Aph-1alpha Presenilin-stabilization factor). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-247aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 42.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eAPH1a has been annotated as Non-catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: APH1a — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=APH1a\n- NCBI Gene search: APH1a — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=APH1a\n- Ensembl search: APH1a — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=APH1a\n- AlphaFold DB search: APH1a — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/APH1a\n- RCSB PDB search: APH1a — RCSB PDB — https:\/\/www.rcsb.org\/search?query=APH1a\n- PubMed search: APH1a transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=APH1a+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322984813,"sku":"CSB-CF853390HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592261485,"sku":"CSB-CF853390HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF853390HU-SDS.jpg?v=1778623121"},{"product_id":"recombinant-human-herpesvirus-6b-protein-u22-u22-bhp10508125","title":"Recombinant Human herpesvirus 6B Protein U22 (U22)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic virus): Human herpesvirus 6B Protein U22 (U22) corresponding to amino acids 1–202. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–202 (202 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 2TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic virus). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q9QJ44. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman herpesvirus 6B Protein U22 (U22) is a membrane-associated protein from Human herpesvirus 6B. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human herpesvirus 6B Protein U22 (U22) (Q9QJ44) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q9QJ44\/entry\n- NCBI Gene search: U22 Human herpesvirus 6B — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=U22%20Human%20herpesvirus%206B\n- PubMed search: U22 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=U22%20review\n- InterPro search: U22 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/U22\/\n- Ensembl Gene Summary: U22 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=U22\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322952045,"sku":"CSB-CF889529HKA-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591507821,"sku":"CSB-CF889529HKA-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF889529HKA-SDS.jpg?v=1778623114"},{"product_id":"recombinant-sindbis-virus-structural-polyprotein-partial-bhp10505930","title":"Recombinant Sindbis virus Structural polyprotein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eRecombinant Sindbis virus Structural polyprotein, partial\u003c\/strong\u003e (also reported as p130) from Sindbis virus (SINV). In the supplied product notes, the target is described as \u003cem\u003eCapsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Recombinant Sindbis virus Structural polyprotein, partial (also reported as p130). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 807-1245aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 65.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eRecombinant Sindbis virus Structural polyprotein, partial has been annotated as Capsid protein. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Recombinant Sindbis virus Structural polyprotein, partial — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- NCBI Gene search: Recombinant Sindbis virus Structural polyprotein, partial — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- Ensembl search: Recombinant Sindbis virus Structural polyprotein, partial — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- AlphaFold DB search: Recombinant Sindbis virus Structural polyprotein, partial — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- RCSB PDB search: Recombinant Sindbis virus Structural polyprotein, partial — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial\n- PubMed search: Recombinant Sindbis virus Structural polyprotein, partial transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Recombinant+Sindbis+virus+Structural+polyprotein%2C+partial+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323017581,"sku":"CSB-CF361018SHZb2-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320591278445,"sku":"CSB-CF361018SHZb2-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF361018SHZb2-SDS.jpg?v=1778623117"},{"product_id":"recombinant-human-olfactory-receptor-5v1-or5v1-bhp10507091","title":"Recombinant Human Olfactory receptor 5V1 (OR5V1)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Homo sapiens (Human): Human Olfactory receptor 5V1 (OR5V1) corresponding to amino acids 1–321. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–321 (321 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q9UGF6. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Olfactory receptor 5V1 (OR5V1) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: Hs6M1-21 (Olfactory receptor OR6-26).\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Olfactory receptor 5V1 (OR5V1) (Q9UGF6) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q9UGF6\/entry\n- NCBI Gene search: OR5V1 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=OR5V1%20Homo%20sapiens\n- PubMed search: OR5V1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=OR5V1%20review\n- InterPro search: OR5V1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/OR5V1\/\n- Ensembl Gene Summary: OR5V1 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=OR5V1\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323050349,"sku":"CSB-CF871401HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592163181,"sku":"CSB-CF871401HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF871401HU-SDS.jpg?v=1778623121"},{"product_id":"recombinant-human-metalloreductase-steap2-steap2-bhp10505918","title":"Recombinant Human Metalloreductase STEAP2 (STEAP2)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eSTEAP2\u003c\/strong\u003e (also reported as Prostate cancer-associated protein 1 Protein up-regulated in metastatic prostate cancer) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eMetalloreductase that has the ability to reduce both Fe3+ to Fe2+ and Cu2+ to Cu1+.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e STEAP2 (also reported as Prostate cancer-associated protein 1 Protein up-regulated in metastatic prostate cancer). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-490aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 74.6 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eSTEAP2 has been annotated as Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor (By similarity).. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: STEAP2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=STEAP2\n- NCBI Gene search: STEAP2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=STEAP2\n- Ensembl search: STEAP2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=STEAP2\n- AlphaFold DB search: STEAP2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/STEAP2\n- RCSB PDB search: STEAP2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=STEAP2\n- PubMed search: STEAP2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=STEAP2+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323214189,"sku":"CSB-CF854119HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588788077,"sku":"CSB-CF854119HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF854119HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-g-protein-coupled-receptor-family-c-group-5-member-d-gprc5d-bhp10508132","title":"Recombinant Human G-protein coupled receptor family C group 5 member D (GPRC5D)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Homo sapiens (Human): Human G-protein coupled receptor family C group 5 member D (GPRC5D) corresponding to amino acids 1–345. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–345 (345 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q9NZD1. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman G-protein coupled receptor family C group 5 member D (GPRC5D) is described as a G protein-coupled receptor (GPCR), a large family of multi-pass membrane proteins that couple extracellular cues to intracellular signaling through heterotrimeric G proteins and other effectors. Many GPCRs are 'orphan' receptors with incompletely defined endogenous ligands, making them active areas for receptor deorphanization and chemical biology. Because GPCRs are conformationally dynamic and embedded in membranes, constructs and display formats can influence epitope accessibility and functional readouts.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eDeorphanization and ligand discovery using high-throughput signaling assays, β-arrestin recruitment, and chemoproteomic approaches.\u003c\/li\u003e\n\u003cli\u003eStructure-guided GPCR research (cryo-EM and stabilized constructs) to map active\/inactive conformations and allosteric sites.\u003c\/li\u003e\n\u003cli\u003eBiased signaling and receptor trafficking studies that connect distinct signaling pathways to specific cellular phenotypes.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntibody or binder generation against extracellular loops\/domains to support receptor detection and localization studies.\u003c\/li\u003e\n\u003cli\u003eIn vitro binding or interaction studies (e.g., ligand\/binder screening) where defined receptor fragments or displayed receptors aid comparability.\u003c\/li\u003e\n\u003cli\u003eCell biology studies of receptor expression, internalization, and pathway activation in engineered systems (interpretation focused, no protocols).\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human G-protein coupled receptor family C group 5 member D (GPRC5D) (Q9NZD1) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q9NZD1\/entry\n- NCBI Gene search: GPRC5D Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=GPRC5D%20Homo%20sapiens\n- PubMed search: GPRC5D review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=GPRC5D%20review\n- InterPro search: GPRC5D — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/GPRC5D\/\n- Ensembl Gene Summary: GPRC5D (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=GPRC5D\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n- Guide to PHARMACOLOGY (GPCR resource) — IUPHAR\/BPS — https:\/\/www.guidetopharmacology.org\/\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323083117,"sku":"CSB-CF882153HU-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590819693,"sku":"CSB-CF882153HU-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF882153HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-varicella-zoster-virus-envelope-glycoprotein-e-ge-bhp10505941","title":"Recombinant Varicella-zoster virus Envelope glycoprotein E (gE)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003egE\u003c\/strong\u003e (also reported as gE; ORF68Envelope glycoprotein E; gE) from Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3). In the supplied product notes, the target is described as \u003cem\u003eEnvelope glycoprotein that binds to the potential host cell entry receptor IDE.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e gE (also reported as gE; ORF68Envelope glycoprotein E; gE). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 31-623aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 85.4 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003egE has been annotated as Envelope glycoprotein that binds to the potential host cell entry receptor IDE.; FUNCTION. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: gE — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=gE\n- NCBI Gene search: gE — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=gE\n- Ensembl search: gE — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=gE\n- AlphaFold DB search: gE — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/gE\n- RCSB PDB search: gE — RCSB PDB — https:\/\/www.rcsb.org\/search?query=gE\n- PubMed search: gE transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=gE+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323115885,"sku":"CSB-CF362630VAP-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590524781,"sku":"CSB-CF362630VAP-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF362630VAP-SDS.jpg?v=1778623117"},{"product_id":"recombinant-rat-micos-complex-subunit-mic60-immt-partial-bhp10507085","title":"Recombinant Rat MICOS complex subunit Mic60 (Immt), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eImmt\u003c\/strong\u003e (also reported as Mitochondrial inner membrane protein (Mitofilin) (Mic60)) from Rattus norvegicus (Rat). In the supplied product notes, the target is described as \u003cem\u003eComponent of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to…\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Immt (also reported as Mitochondrial inner membrane protein (Mitofilin) (Mic60)). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 34-609aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 66.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eImmt is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Immt — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Immt\n- NCBI Gene search: Immt — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Immt\n- Ensembl search: Immt — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Immt\n- AlphaFold DB search: Immt — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Immt\n- RCSB PDB search: Immt — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Immt\n- PubMed search: Immt transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Immt+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323148653,"sku":"CSB-CF665982RA-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320593604973,"sku":"CSB-CF665982RA-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF665982RA-SDS.jpg?v=1778623123"},{"product_id":"recombinant-human-glycophorin-b-gypb-bhp10508400","title":"Recombinant Human Glycophorin-B (GYPB)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Homo sapiens (Human): Human Glycophorin-B (GYPB) corresponding to amino acids 20–91. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 20–91 (72 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 1TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P06028. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Glycophorin-B (GYPB) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: PAS-3; SS-active sialoglycoprotein; Sialoglycoprotein delta; CD_antigen: CD235b.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Glycophorin-B (GYPB) (P06028) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P06028\/entry\n- NCBI Gene search: GYPB Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=GYPB%20Homo%20sapiens\n- PubMed search: GYPB review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=GYPB%20review\n- InterPro search: GYPB — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/GYPB\/\n- Ensembl Gene Summary: GYPB (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=GYPB\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323181421,"sku":"CSB-CF010075HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592458093,"sku":"CSB-CF010075HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF010075HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-nipah-virus-glycoprotein-g-g-bhp10505916","title":"Recombinant Nipah virus Glycoprotein G (G)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eG\u003c\/strong\u003e (also reported as GGlycoprotein G) from Nipah virus. In the supplied product notes, the target is described as \u003cem\u003eInteracts with host ephrinB2\/EFNB2 or ephrin B3\/EFNB3 to provide virion attachment to target cell.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e G (also reported as GGlycoprotein G). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-602aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 72 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eG has been annotated as Interacts with host ephrinB2\/EFNB2 or ephrin B3\/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: G — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=G\n- NCBI Gene search: G — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=G\n- Ensembl search: G — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=G\n- AlphaFold DB search: G — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/G\n- RCSB PDB search: G — RCSB PDB — https:\/\/www.rcsb.org\/search?query=G\n- PubMed search: G transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=G+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323279725,"sku":"CSB-CF862323NDT-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590098797,"sku":"CSB-CF862323NDT-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF862323NDT-SDS.jpg?v=1778623124"},{"product_id":"recombinant-human-atp-sensitive-inward-rectifier-potassium-channel-10-kcnj10-bhp10503913","title":"Recombinant Human ATP-sensitive inward rectifier potassium channel 10 (KCNJ10)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eKCNJ10\u003c\/strong\u003e (also reported as ATP-dependent inwardly rectifying potassium channel Kir4.1 Inward rectifier K(+) channel Kir1.2 Potassium channel, inwardly rectifying subfamily J member 10) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eMay be responsible for potassium buffering action of glial cells in the brain.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e KCNJ10 (also reported as ATP-dependent inwardly rectifying potassium channel Kir4.1 Inward rectifier K(+) channel Kir1.2 Potassium channel, inwardly rectifying subfamily J member 10). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-379aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 58.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eKCNJ10 has been annotated as May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: KCNJ10 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=KCNJ10\n- NCBI Gene search: KCNJ10 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=KCNJ10\n- Ensembl search: KCNJ10 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=KCNJ10\n- AlphaFold DB search: KCNJ10 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/KCNJ10\n- RCSB PDB search: KCNJ10 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=KCNJ10\n- PubMed search: KCNJ10 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=KCNJ10+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323312493,"sku":"CSB-CF012048HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588624237,"sku":"CSB-CF012048HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF012048HU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-guinea-pig-voltage-dependent-l-type-calcium-channel-subunit-alpha-1c-cacna1c-partial-bhp10508133","title":"Recombinant Guinea pig Voltage-dependent L-type calcium channel subunit alpha-1C (CACNA1C), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCACNA1C\u003c\/strong\u003e (also reported as Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle Voltage-gated calcium channel subunit alpha Cav1.2) from Cavia porcellus (Guinea pig). In the supplied product notes, the target is described as \u003cem\u003ePore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CACNA1C (also reported as Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle Voltage-gated calcium channel subunit alpha Cav1.2). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-169aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 22.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCACNA1C is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CACNA1C — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CACNA1C\n- NCBI Gene search: CACNA1C — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CACNA1C\n- Ensembl search: CACNA1C — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CACNA1C\n- AlphaFold DB search: CACNA1C — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CACNA1C\n- RCSB PDB search: CACNA1C — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CACNA1C\n- PubMed search: CACNA1C transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CACNA1C+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323246957,"sku":"CSB-CF004399GU-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592753005,"sku":"CSB-CF004399GU-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF004399GU-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-platelet-glycoprotein-ib-beta-chain-gp1bb-bhp10505933","title":"Recombinant Human Platelet glycoprotein Ib beta chain (GP1BB)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eGP1BB\u003c\/strong\u003e (also reported as Antigen CD42b-beta CD_antigen: CD42c) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eGp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e GP1BB (also reported as Antigen CD42b-beta CD_antigen: CD42c). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 26-206aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 39.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eGP1BB has been annotated as Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: GP1BB — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=GP1BB\n- NCBI Gene search: GP1BB — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=GP1BB\n- Ensembl search: GP1BB — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=GP1BB\n- AlphaFold DB search: GP1BB — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/GP1BB\n- RCSB PDB search: GP1BB — RCSB PDB — https:\/\/www.rcsb.org\/search?query=GP1BB\n- PubMed search: GP1BB transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=GP1BB+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323345261,"sku":"CSB-CF009686HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320589836653,"sku":"CSB-CF009686HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF009686HU-SDS.jpg?v=1778623116"},{"product_id":"recombinant-human-androgen-dependent-tfpi-regulating-protein-adtrp-bhp10505914","title":"Recombinant Human Androgen-dependent TFPI-regulating protein (ADTRP)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eADTRP\u003c\/strong\u003e (also reported as C6orf105) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eRegulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e ADTRP (also reported as C6orf105). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-230aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 46.8 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eADTRP has been annotated as Regulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells (in vitro).. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: ADTRP — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ADTRP\n- NCBI Gene search: ADTRP — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ADTRP\n- Ensembl search: ADTRP — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ADTRP\n- AlphaFold DB search: ADTRP — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ADTRP\n- RCSB PDB search: ADTRP — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ADTRP\n- PubMed search: ADTRP transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ADTRP+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323443565,"sku":"CSB-CF846640HUb3-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320589803885,"sku":"CSB-CF846640HUb3-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF846640HUb3-SDS.jpg?v=1778623122"},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-6-ccr6-bhp10505940","title":"Recombinant Human C-C chemokine receptor type 6 (CCR6)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCCR6\u003c\/strong\u003e (also reported as Chemokine receptor-like 3) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for the C-C type chemokine CCL20.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CCR6 (also reported as Chemokine receptor-like 3). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-374aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 58.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCCR6 has been annotated as Receptor for the C-C type chemokine CCL20. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: CCR6 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CCR6\n- NCBI Gene search: CCR6 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR6\n- Ensembl search: CCR6 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CCR6\n- AlphaFold DB search: CCR6 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CCR6\n- RCSB PDB search: CCR6 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CCR6\n- PubMed search: CCR6 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR6+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323378029,"sku":"CSB-CF004845HUa2-100UG","price":1700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320590557549,"sku":"CSB-CF004845HUa2-20UG","price":1040.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF004845HUa2-SDS.jpg?v=1778623117"},{"product_id":"recombinant-human-cation-dependent-mannose-6-phosphate-receptor-m6pr-bhp10508839","title":"Recombinant Human Cation-dependent mannose-6-phosphate receptor (M6PR)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Homo sapiens (Human): Human Cation-dependent mannose-6-phosphate receptor (M6PR) corresponding to amino acids 27–277. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 27–277 (251 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 1TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P20645. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Cation-dependent mannose-6-phosphate receptor (M6PR) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: 46 kDa mannose 6-phosphate receptor （MPR 46）.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Cation-dependent mannose-6-phosphate receptor (M6PR) (P20645) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P20645\/entry\n- NCBI Gene search: M6PR Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=M6PR%20Homo%20sapiens\n- PubMed search: M6PR review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=M6PR%20review\n- InterPro search: M6PR — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/M6PR\/\n- Ensembl Gene Summary: M6PR (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=M6PR\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323410797,"sku":"CSB-CF013293HU-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320592785773,"sku":"CSB-CF013293HU-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF013293HU-SDS.jpg?v=1778623119"},{"product_id":"recombinant-mouse-bcl2-adenovirus-e1b-19-kda-protein-interacting-protein-3-bnip3-partial-bhp10505999","title":"Recombinant Mouse BCL2\/adenovirus E1B 19 kDa protein-interacting protein 3 (Bnip3), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eBnip3\u003c\/strong\u003e (also reported as Nip3) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003eApoptosis-inducing protein that can overcome BCL2 suppression.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e Bnip3 (also reported as Nip3). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 50-187aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 21.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eBnip3 has been annotated as Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18\/MIEAP. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: Bnip3 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Bnip3\n- NCBI Gene search: Bnip3 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Bnip3\n- Ensembl search: Bnip3 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Bnip3\n- AlphaFold DB search: Bnip3 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Bnip3\n- RCSB PDB search: Bnip3 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Bnip3\n- PubMed search: Bnip3 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Bnip3+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207323476333,"sku":"CSB-CF002766MO2-100UG","price":1420.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320593146221,"sku":"CSB-CF002766MO2-20UG","price":878.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF002766MO2-SDS.jpg?v=1778623120"}],"url":"https:\/\/www.ebiohippo.com\/collections\/transmembrane-proteins.oembed","provider":"BioHippo","version":"1.0","type":"link"}