{"title":"Detergent-Solubilized Membrane Proteins","description":"Recombinant membrane proteins purified in detergent micelles — the broadest, most established format for structural and biochemical work.","products":[{"product_id":"recombinant-human-b-lymphocyte-antigen-cd20-ms4a1-detergent-active-bhp10513346","title":"Recombinant Human B-lymphocyte antigen CD20 (MS4A1)-Detergent (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMS4A1\u003c\/strong\u003e (also reported as (B-lymphocyte surface antigen B1) (Bp35) (Leukocyte surface antigen Leu-16) (Membrane-spanning 4-domains subfamily A member 1) (CD20)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eB-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes (PubMed:3925015, PubMed:7684739, PubMe…\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 MS4A1 (also reported as (B-lymphocyte surface antigen B1) (Bp35) (Leukocyte surface antigen Leu-16) (Membrane-spanning 4-domains subfamily A member 1) (CD20)). 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 1-297aa. 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 Mammalian cell. 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; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 34.4 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eMS4A1 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: MS4A1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=MS4A1\n- NCBI Gene search: MS4A1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MS4A1\n- Ensembl search: MS4A1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=MS4A1\n- AlphaFold DB search: MS4A1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/MS4A1\n- RCSB PDB search: MS4A1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=MS4A1\n- PubMed search: MS4A1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MS4A1+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207336452461,"sku":"CSB-MP015007HU-D-1MG","price":10098.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320608121197,"sku":"CSB-MP015007HU-D-100UG","price":2687.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320608153965,"sku":"CSB-MP015007HU-D-20UG","price":725.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP015007HU-D-SDS.jpg?v=1778623231"},{"product_id":"recombinant-human-claudin-18-2-cldn18-2-detergent-active-bhp10513345","title":"Recombinant Human Claudin-18.2 (CLDN18.2)-Detergent (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN18.2\u003c\/strong\u003e (also reported as (CLDN18.2)) 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, through calcium-independent cell-adhesion activity.\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 CLDN18.2 (also reported as (CLDN18.2)). 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 1-261aa. 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 Mammalian cell. 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; purity: Greater than 80% as determined by SDS-PAGE.; molecular weight: 29.1 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN18.2 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: CLDN18.2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN18.2\n- NCBI Gene search: CLDN18.2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN18.2\n- Ensembl search: CLDN18.2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN18.2\n- AlphaFold DB search: CLDN18.2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN18.2\n- RCSB PDB search: CLDN18.2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN18.2\n- PubMed search: CLDN18.2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN18.2+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207336845677,"sku":"CSB-MP005498HU(A5)-D-1MG","price":7410.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320607957357,"sku":"CSB-MP005498HU(A5)-D-100UG","price":1395.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320607990125,"sku":"CSB-MP005498HU(A5)-D-20UG","price":684.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005498HU_A5_-D-SDS.jpg?v=1778623158"},{"product_id":"recombinant-human-claudin-6-cldn6-detergent-active-bhp10513923","title":"Recombinant Human Claudin-6 (CLDN6)-Detergent (Active)","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 UNQ757; PRO1488) 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.\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 UNQ757; PRO1488). 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 2-220aa. 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 Mammalian cell. 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: 27.7 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN6 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: 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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207338484077,"sku":"CSB-MP005508HU(A5)-D-1MG","price":10098.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320610808173,"sku":"CSB-MP005508HU(A5)-D-100UG","price":2687.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320610840941,"sku":"CSB-MP005508HU(A5)-D-20UG","price":725.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005508HU_A5_-D-SDS.jpg?v=1778623167"},{"product_id":"recombinant-human-solute-carrier-family-23-member-2-slc23a2-detergent-bhp10514880","title":"Recombinant Human Solute carrier family 23 member 2 (SLC23A2)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eSLC23A2\u003c\/strong\u003e (also reported as Na(+)\/L-ascorbic acid transporter 2;Nucleobase transporter-like 1 protein;Sodium-dependent vitamin C transporter 2 ;Yolk sac permease-like molecule 2) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eSodium\/ascorbate cotransporter .\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 SLC23A2 (also reported as Na(+)\/L-ascorbic acid transporter 2;Nucleobase transporter-like 1 protein;Sodium-dependent vitamin C transporter 2 ;Yolk sac permease-like molecule 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 1-650aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 71.2 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eSLC23A2 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: SLC23A2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=SLC23A2\n- NCBI Gene search: SLC23A2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=SLC23A2\n- Ensembl search: SLC23A2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=SLC23A2\n- AlphaFold DB search: SLC23A2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/SLC23A2\n- RCSB PDB search: SLC23A2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=SLC23A2\n- PubMed search: SLC23A2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SLC23A2+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207340122477,"sku":"CSB-MP866221HU(A4)-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320614740333,"sku":"CSB-MP866221HU(A4)-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320614773101,"sku":"CSB-MP866221HU(A4)-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP866221HU_A4_-D-SDS.jpg?v=1778623175"},{"product_id":"recombinant-humanreceptor-type-tyrosine-protein-phosphatase-alpha-ptpra-detergent-bhp10515243","title":"Recombinant HumanReceptor-type tyrosine-protein phosphatase alpha (PTPRA)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003ePTPRA\u003c\/strong\u003e (also reported as Protein-tyrosine phosphatase alpha;R-PTP-alpha;EC 3.1.3.48) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eTyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation.\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 PTPRA (also reported as Protein-tyrosine phosphatase alpha;R-PTP-alpha;EC 3.1.3.48). 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 20-802aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 93.1 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ePTPRA 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: PTPRA — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=PTPRA\n- NCBI Gene search: PTPRA — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=PTPRA\n- Ensembl search: PTPRA — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=PTPRA\n- AlphaFold DB search: PTPRA — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/PTPRA\n- RCSB PDB search: PTPRA — RCSB PDB — https:\/\/www.rcsb.org\/search?query=PTPRA\n- PubMed search: PTPRA transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=PTPRA+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207340777837,"sku":"CSB-MP019047HU-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320615035245,"sku":"CSB-MP019047HU-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320615068013,"sku":"CSB-MP019047HU-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP019047HU-D-SDS.jpg?v=1778623175"},{"product_id":"recombinant-human-5-hydroxytryptamine-receptor-3a-htr3a-biotinylated-detergent-bhp10515241","title":"Recombinant Human 5-hydroxytryptamine receptor 3A (HTR3A), Biotinylated-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHTR3A\u003c\/strong\u003e (also reported as 5-HT3-A;5-HT3A;5-hydroxytryptamine receptor 3;5-HT-3;5-HT3R;Serotonin receptor 3A;Serotonin-gated ion channel receptor) 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 HTR3A (also reported as 5-HT3-A;5-HT3A;5-hydroxytryptamine receptor 3;5-HT-3;5-HT3R;Serotonin receptor 3A;Serotonin-gated ion channel 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 24-478aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 59.8 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHTR3A 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: HTR3A — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HTR3A\n- NCBI Gene search: HTR3A — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HTR3A\n- Ensembl search: HTR3A — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HTR3A\n- AlphaFold DB search: HTR3A — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HTR3A\n- RCSB PDB search: HTR3A — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HTR3A\n- PubMed search: HTR3A transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HTR3A+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207340941677,"sku":"CSB-MP010890HU-B-D-1MG","price":10217.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320615723373,"sku":"CSB-MP010890HU-B-D-100UG","price":2090.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320615756141,"sku":"CSB-MP010890HU-B-D-20UG","price":1145.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP010890HU-B-D-SDS.jpg?v=1778623171"},{"product_id":"recombinant-mouse-1-acyl-sn-glycerol-3-phosphate-acyltransferase-beta-agpat2-detergent-bhp10514708","title":"Recombinant Mouse 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (Agpat2)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eAgpat2\u003c\/strong\u003e (also reported as 1-acylglycerol-3-phosphate O-acyltransferase 2;1-AGP acyltransferase 2;1-AGPAT 2;Lysophosphatidic acid acyltransferase beta;LPAAT-beta) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003eConverts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.\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 Agpat2 (also reported as 1-acylglycerol-3-phosphate O-acyltransferase 2;1-AGP acyltransferase 2;1-AGPAT 2;Lysophosphatidic acid acyltransferase beta;LPAAT-beta). 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 24-278aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 32.8 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eAgpat2 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: Agpat2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Agpat2\n- NCBI Gene search: Agpat2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Agpat2\n- Ensembl search: Agpat2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Agpat2\n- AlphaFold DB search: Agpat2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Agpat2\n- RCSB PDB search: Agpat2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Agpat2\n- PubMed search: Agpat2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Agpat2+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207341039981,"sku":"CSB-MP814318MO-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320613364077,"sku":"CSB-MP814318MO-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320613396845,"sku":"CSB-MP814318MO-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP814318MO-D-SDS.jpg?v=1778623170"},{"product_id":"recombinant-oryza-glumipatula-citrate-transporter-like-domain-containing-protein-detergent-bhp10515333","title":"Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Oryza glumipatula: Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent (Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent) corresponding to amino acids 1–472. 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 1–472 (472 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 9TM. 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 Mammalian cell. Mammalian expression can support more native-like folding and post-translational modifications for complex membrane proteins, which may be important for conformation-sensitive binding studies.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Oryza glumipatula. 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 A0A0D9Z0W3. 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 glumipatula Citrate transporter-like domain-containing protein-Detergent (Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent) is a membrane-associated protein from Oryza glumipatula. 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 Mammalian expression can support native-like disulfide formation and post-translational processing, which may help preserve conformational epitopes for multi-pass membrane proteins. Even so, region boundaries and membrane context remain important for interpreting binding and functional readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent (Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent) (A0A0D9Z0W3) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/A0A0D9Z0W3\/entry\n- NCBI Gene search: Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent Oryza glumipatula — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Recombinant%20Oryza%20glumipatula%20Citrate%20transporter-like%20domain-containing%20protein-Detergent%20Oryza%20glumipatula\n- PubMed search: Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Recombinant%20Oryza%20glumipatula%20Citrate%20transporter-like%20domain-containing%20protein-Detergent%20review\n- InterPro search: Recombinant Oryza glumipatula Citrate transporter-like domain-containing protein-Detergent — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/Recombinant%20Oryza%20glumipatula%20Citrate%20transporter-like%20domain-containing%20protein-Detergent\/\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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207341367661,"sku":"CSB-MP6061GYIm12-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320616018285,"sku":"CSB-MP6061GYIm12-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320616051053,"sku":"CSB-MP6061GYIm12-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP6061GYIm12-D-SDS.jpg?v=1778623174"},{"product_id":"recombinant-human-claudin-4-cldn4-detergent-bhp10515254","title":"Recombinant Human Claudin-4 (CLDN4)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN4\u003c\/strong\u003e (also reported as Clostridium perfringens enterotoxin receptor;CPE-R;CPE-receptor;Williams-Beuren syndrome chromosomal region 8 protein) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eChannel-forming tight junction protein that mediates paracellular chloride transport in the kidney.\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 CLDN4 (also reported as Clostridium perfringens enterotoxin receptor;CPE-R;CPE-receptor;Williams-Beuren syndrome chromosomal region 8 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 1-209aa. 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 Mammalian cell. 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; purity: Greater than 95% as determined by SDS-PAGE.; molecular weight: 26.6 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN4 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: CLDN4 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN4\n- NCBI Gene search: CLDN4 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN4\n- Ensembl search: CLDN4 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN4\n- AlphaFold DB search: CLDN4 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN4\n- RCSB PDB search: CLDN4 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN4\n- PubMed search: CLDN4 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN4+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207341793645,"sku":"CSB-MP005506HU-D-1MG","price":10098.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320615362925,"sku":"CSB-MP005506HU-D-100UG","price":2687.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320615395693,"sku":"CSB-MP005506HU-D-20UG","price":725.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005506HU-D-SDS.jpg?v=1778623172"},{"product_id":"recombinant-human-claudin-9-cldn9-partial-detergent-active-bhp10515364","title":"Recombinant Human Claudin-9 (CLDN9), partial-Detergent (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN9\u003c\/strong\u003e (also reported as Claudin-9; CLDN9) 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, through calcium-independent cell-adhesion activity.\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 CLDN9 (also reported as Claudin-9; CLDN9). 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 2-217aa. 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 Mammalian cell. 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; purity: Greater than 95% as determined by SDS-PAGE.; molecular weight: 27.3 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN9 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: CLDN9 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN9\n- NCBI Gene search: CLDN9 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN9\n- Ensembl search: CLDN9 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN9\n- AlphaFold DB search: CLDN9 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN9\n- RCSB PDB search: CLDN9 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN9\n- PubMed search: CLDN9 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN9+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207341826413,"sku":"CSB-MP005511HU1-D-1MG","price":10098.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320616575341,"sku":"CSB-MP005511HU1-D-100UG","price":2687.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320616608109,"sku":"CSB-MP005511HU1-D-20UG","price":725.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005511HU1-D-SDS_ebbdee38-7c5c-4c84-83e9-2a1ff0b1d698.jpg?v=1778623175"},{"product_id":"recombinant-human-long-chain-fatty-acid-coa-ligase-1-acsl1-detergent-bhp10516551","title":"Recombinant Human Long-chain-fatty-acid--CoA ligase 1 (ACSL1)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eACSL1\u003c\/strong\u003e (also reported as Acyl-CoA synthetase 1;Arachidonate--CoA ligase;Long-chain acyl-CoA synthetase 1;Long-chain acyl-CoA synthetase 2;Long-chain fatty acid-CoA ligase 2;Palmitoyl-CoA ligase 1;Palmitoyl-CoA ligase 2;Phytanate--CoA ligase) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eCatalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.\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 ACSL1 (also reported as Acyl-CoA synthetase 1;Arachidonate--CoA ligase;Long-chain acyl-CoA synthetase 1;Long-chain acyl-CoA synthetase 2;Long-chain fatty acid-CoA ligase 2;Palmitoyl-CoA ligase 1;Palmitoyl-CoA ligase 2;Phytanate--CoA ligase). 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 1-698aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 81.4 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eACSL1 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: ACSL1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ACSL1\n- NCBI Gene search: ACSL1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ACSL1\n- Ensembl search: ACSL1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ACSL1\n- AlphaFold DB search: ACSL1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ACSL1\n- RCSB PDB search: ACSL1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ACSL1\n- PubMed search: ACSL1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ACSL1+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207344480621,"sku":"CSB-MP001191HU-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320620179821,"sku":"CSB-MP001191HU-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320620212589,"sku":"CSB-MP001191HU-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP001191HU-D-SDS.jpg?v=1778623186"},{"product_id":"recombinant-human-long-chain-fatty-acid-coa-ligase-1-acsl1-detergent-bhp10516552","title":"Recombinant Human Long-chain-fatty-acid--CoA ligase 1 (ACSL1)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eACSL1\u003c\/strong\u003e (also reported as Acyl-CoA synthetase 1;Arachidonate--CoA ligase;Long-chain acyl-CoA synthetase 1;Long-chain acyl-CoA synthetase 2;Long-chain fatty acid-CoA ligase 2;Palmitoyl-CoA ligase 1;Palmitoyl-CoA ligase 2;Phytanate--CoA ligase) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eCatalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.\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 ACSL1 (also reported as Acyl-CoA synthetase 1;Arachidonate--CoA ligase;Long-chain acyl-CoA synthetase 1;Long-chain acyl-CoA synthetase 2;Long-chain fatty acid-CoA ligase 2;Palmitoyl-CoA ligase 1;Palmitoyl-CoA ligase 2;Phytanate--CoA ligase). 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 1-698aa. 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 Mammalian cell. 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; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 82.1 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eACSL1 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: ACSL1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ACSL1\n- NCBI Gene search: ACSL1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ACSL1\n- Ensembl search: ACSL1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ACSL1\n- AlphaFold DB search: ACSL1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ACSL1\n- RCSB PDB search: ACSL1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ACSL1\n- PubMed search: ACSL1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ACSL1+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207344578925,"sku":"CSB-MP001191HUq3-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320620245357,"sku":"CSB-MP001191HUq3-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320620278125,"sku":"CSB-MP001191HUq3-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP001191HUq3-D-SDS.jpg?v=1778623185"},{"product_id":"recombinant-human-claudin-1-cldn1-detergent-active-bhp10516621","title":"Recombinant Human Claudin-1 (CLDN1)-Detergent (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN1\u003c\/strong\u003e (also reported as Senescence-associated epithelial membrane protein; CLDN1; CLD1, SEMP1; UNQ481\/PRO944) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eClaudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia.\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 CLDN1 (also reported as Senescence-associated epithelial membrane protein; CLDN1; CLD1, SEMP1; UNQ481\/PRO944). 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 2-211aa. 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 Mammalian cell. 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: 25.1 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN1 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: CLDN1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN1\n- NCBI Gene search: CLDN1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN1\n- Ensembl search: CLDN1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN1\n- AlphaFold DB search: CLDN1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN1\n- RCSB PDB search: CLDN1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN1\n- PubMed search: CLDN1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN1+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207344939373,"sku":"CSB-MP005490HU1-D-1MG","price":10098.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320620310893,"sku":"CSB-MP005490HU1-D-100UG","price":2687.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320620343661,"sku":"CSB-MP005490HU1-D-20UG","price":725.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005490HU1-D-SDS.jpg?v=1778623187"},{"product_id":"recombinant-human-claudin-18-2-cldn18-2-detergent-bhp10516622","title":"Recombinant Human Claudin-18.2 (CLDN18.2)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN18.2\u003c\/strong\u003e (also reported as CLDN18;UNQ778\/PRO1572) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eRequired for the formation of the gastric paracellular barrier via its role in tight junction formation, thereby involved in the response to gastric acidification\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 CLDN18.2 (also reported as CLDN18;UNQ778\/PRO1572). 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 1-261aa. 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 Mammalian cell. 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; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 32.0 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCLDN18.2 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: CLDN18.2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN18.2\n- NCBI Gene search: CLDN18.2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN18.2\n- Ensembl search: CLDN18.2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN18.2\n- AlphaFold DB search: CLDN18.2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN18.2\n- RCSB PDB search: CLDN18.2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN18.2\n- PubMed search: CLDN18.2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN18.2+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207345234285,"sku":"CSB-MP005498HU(A5)q3-D-1MG","price":7410.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320621064557,"sku":"CSB-MP005498HU(A5)q3-D-100UG","price":1395.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320621097325,"sku":"CSB-MP005498HU(A5)q3-D-20UG","price":684.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005498HU_A5_q3-D-SDS.jpg?v=1778623186"},{"product_id":"recombinant-human-bdnf-nt-3-growth-factors-receptor-ntrk2-detergent-bhp10516940","title":"Recombinant Human BDNF\/NT-3 growth factors receptor (NTRK2)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eNTRK2\u003c\/strong\u003e (also reported as GP145-TrkB (Trk-B);Neurotrophic tyrosine kinase receptor type 2;TrkB tyrosine kinase;Tropomyosin-related kinase B) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse form…\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 NTRK2 (also reported as GP145-TrkB (Trk-B);Neurotrophic tyrosine kinase receptor type 2;TrkB tyrosine kinase;Tropomyosin-related kinase B). 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 32-822aa. 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 Mammalian cell. 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; purity: Greater than 90% as determined by SDS-PAGE.; molecular weight: 89.7 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eNTRK2 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\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: NTRK2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=NTRK2\n- NCBI Gene search: NTRK2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=NTRK2\n- Ensembl search: NTRK2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=NTRK2\n- AlphaFold DB search: NTRK2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/NTRK2\n- RCSB PDB search: NTRK2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=NTRK2\n- PubMed search: NTRK2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=NTRK2+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207345398125,"sku":"CSB-MP619082HU(A4)-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320622408045,"sku":"CSB-MP619082HU(A4)-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320622440813,"sku":"CSB-MP619082HU(A4)-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP619082HU_A4_-D-SDS.jpg?v=1778623188"},{"product_id":"recombinant-human-somatostatin-receptor-type-2-sstr2-detergent-bhp10516835","title":"Recombinant Human Somatostatin receptor type 2 (SSTR2)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eSSTR2\u003c\/strong\u003e (also reported as SRIF-1) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for somatostatin-14 and -28.\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 SSTR2 (also reported as SRIF-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 1-369aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 48.4 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eSSTR2 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: SSTR2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=SSTR2\n- NCBI Gene search: SSTR2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=SSTR2\n- Ensembl search: SSTR2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=SSTR2\n- AlphaFold DB search: SSTR2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/SSTR2\n- RCSB PDB search: SSTR2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=SSTR2\n- PubMed search: SSTR2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SSTR2+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207345594733,"sku":"CSB-MP022725HU-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320622276973,"sku":"CSB-MP022725HU-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320622309741,"sku":"CSB-MP022725HU-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP022725HU-D-SDS.jpg?v=1778623187"},{"product_id":"recombinant-human-cd44-antigen-cd44-detergent-bhp10516602","title":"Recombinant Human CD44 antigen (CD44)-Detergent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCD44\u003c\/strong\u003e (also reported as CDw44;Epican;Extracellular matrix receptor III;GP90 lymphocyte homing\/adhesion receptor;HUTCH-I;Heparan sulfate proteoglycan;Hermes antigen;Hyaluronate receptor;Phagocytic glycoprotein 1;Phagocytic glycoprotein I) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eCell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment.\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 CD44 (also reported as CDw44;Epican;Extracellular matrix receptor III;GP90 lymphocyte homing\/adhesion receptor;HUTCH-I;Heparan sulfate proteoglycan;Hermes antigen;Hyaluronate receptor;Phagocytic glycoprotein 1;Phagocytic glycoprotein I). 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 21-742aa. 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 Mammalian cell. 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; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 83.6 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. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eCD44 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: CD44 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CD44\n- NCBI Gene search: CD44 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CD44\n- Ensembl search: CD44 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CD44\n- AlphaFold DB search: CD44 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CD44\n- RCSB PDB search: CD44 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CD44\n- PubMed search: CD44 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CD44+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 TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207345922413,"sku":"CSB-MP004938HU(A4)(F1)-D-1MG","price":11220.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320620507501,"sku":"CSB-MP004938HU(A4)(F1)-D-100UG","price":2985.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320620540269,"sku":"CSB-MP004938HU(A4)(F1)-D-20UG","price":805.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP004938HU_A4_F1_-D-SDS.jpg?v=1778623186"}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/collections\/detergent-micelles-workhorse.png?v=1780678141","url":"https:\/\/www.ebiohippo.com\/collections\/detergent-membrane-proteins.oembed","provider":"BioHippo","version":"1.0","type":"link"}