{"title":"VLP Membrane Proteins","description":"Membrane proteins displayed on the surface of virus-like particles — native oligomeric state and a real membrane context for immunization and antibody discovery.","products":[{"product_id":"virus-like-particles-vlps-isotype-control-bhp10512094","title":"Virus-Like Particles (VLPs) isotype control","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eVirus-Like Particles (VLPs) isotype control is a recombinant protein preparation from the indicated source designed for use in assay development, binding studies, and functional characterization. Key attributes such as expression system, expressed region, and affinity tag(s) help researchers match the reagent to specific experimental readouts.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell expression is commonly used for rapid, scalable production. For targets that require glycosylation or other post-translational modifications, consider how a prokaryotic system may affect folding or activity.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s)\/format:\u003c\/strong\u003e Tag-Free tags can support purification and detection in pull-down or binding assays; confirm that the tag position does not interfere with the interaction of interest.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Supplied as Lyophilized powder; select the format that best fits your lab’s handling and aliquoting preferences.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eRecombinant design choices (expression host, fragment boundaries, and tag configuration) help balance yield, solubility, and assay compatibility. Choose conditions and controls that match the recombinant format to your experimental question.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVLPs\u003c\/strong\u003e has been reported to be involved in biological processes relevant to the listed research areas. When interpreting results, consider species context, domain architecture, and whether the recombinant format represents full-length or a defined region.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigen and virulence-factor studies that compare strain- or domain-specific binding and immune recognition.\u003c\/li\u003e\n\u003cli\u003eUse of recombinant proteins as standards for quantitative assays and serology-oriented method development.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eBinding and interaction assays:\u003c\/strong\u003e quantify partner binding and rank conditions using plate-based formats or biophysical methods (SPR\/BLI).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCell-based functional studies:\u003c\/strong\u003e evaluate dose–response and time-course effects in relevant cell systems when the target acts extracellularly or through receptor engagement.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay development:\u003c\/strong\u003e use as a standard, spike-in control, or positive control where consistent specifications are required.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpretation typically relies on relative comparisons (treated vs control, mutant vs wild-type, or dose\/time series) using consistent sample handling and appropriate normalization.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePost-translational modifications:\u003c\/strong\u003e expression system can affect glycosylation and processing; interpret differences cautiously when comparing to native protein.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIsoforms and domains:\u003c\/strong\u003e expressed regions may not capture all isoform-specific features; match fragment boundaries to your assay’s binding site.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eControls:\u003c\/strong\u003e include blank matrix controls, tag-only controls (where relevant), and orthogonal readouts (e.g., WB\/qPCR\/ELISA) to support interpretation.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProt Knowledgebase entry for VLPs — UniProt — https:\/\/www.uniprot.org\/ - NCBI Gene for VLPs — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - RCSB Protein Data Bank — RCSB PDB — https:\/\/www.rcsb.org\/ - PubMed (reviews and primary literature) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/ - Ensembl gene summary — Ensembl — https:\/\/www.ensembl.org\/ --\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059006103917,"sku":"CSB-MP3838-1MG","price":1770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059119808877,"sku":"CSB-MP3838-100UG","price":334.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059119841645,"sku":"CSB-MP3838-20UG","price":134.0,"currency_code":"USD","in_stock":true}]},{"product_id":"virus-like-particles-vlps-isotype-control-bhp10514312","title":"Virus-Like Particles (VLPs) isotype control","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eVirus-Like Particles (VLPs) isotype control is a recombinant protein preparation derived from the listed source organism. It is commonly used as a defined reagent for assay development, binding studies, and analytical controls where consistent protein specifications are required.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell (may influence folding and post-translational modifications).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag\/format:\u003c\/strong\u003e Tag-Free; Lyophilized powder.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpected size:\u003c\/strong\u003e 61.0 kDa (as provided).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e The purity information is not available for VLPs proteins.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eRegion choice, expression system, and tag\/format can influence folding, post-translational modifications, and interaction behavior in downstream assays.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eVLPs is a viral protein target frequently used in serology and antibody discovery workflows, where defined antigens enable consistent comparisons across samples and studies.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigen design and domain selection to better capture neutralizing versus non-neutralizing antibody responses.\u003c\/li\u003e\n\u003cli\u003eHigh-throughput serology and antibody screening using standardized antigens and plate-based formats.\u003c\/li\u003e\n\u003cli\u003eIntegrating binding kinetics with epitope mapping to support variant-aware immunology studies.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eCoat plates with VLPs antigen for ELISA antibody titration (serum\/plasma).\u003c\/li\u003e\n\u003cli\u003eScreen anti-VLPs antibodies by indirect ELISA and immunoblot readouts.\u003c\/li\u003e\n\u003cli\u003eMap antigenic epitopes using VLPs fragments\/domains (in vitro binding assays).\u003c\/li\u003e\n\u003cli\u003eDevelop antigen-capture assays using VLPs as a standard (spike-in controls).\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpret results in the context of the biological system, assay format, and any known domain\/isoform constraints for the target.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigenic proteins may contain immunodominant regions; domain choice can affect assay readouts and cross-reactivity.\u003c\/li\u003e\n\u003cli\u003eInclude relevant negative controls (e.g., unrelated antigens) and dilution series to support interpretation of binding signals.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - PubMed search — NLM: https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=VLPs - Reactome pathway browser — Reactome: https:\/\/reactome.org\/ - InterPro protein family resource — EMBL-EBI: https:\/\/www.ebi.ac.uk\/interpro\/ --\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059254518125,"sku":"CSB-MP3854-C-1MG","price":1770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059355083117,"sku":"CSB-MP3854-C-100UG","price":334.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059355115885,"sku":"CSB-MP3854-C-20UG","price":134.0,"currency_code":"USD","in_stock":true}]},{"product_id":"virus-like-particles-vlps-isotype-control-egfp-fluorescent-bhp10514323","title":"Virus-Like Particles (VLPs) isotype control, EGFP Fluorescent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eVirus-Like Particles (VLPs) isotype control, EGFP Fluorescent is a recombinant protein preparation derived from the listed source organism. It is commonly used as a defined reagent for assay development, binding studies, and analytical controls where consistent protein specifications are required.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell (may influence folding and post-translational modifications).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag\/format:\u003c\/strong\u003e C-terminal EGFP-tagged; Lyophilized powder.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpected size:\u003c\/strong\u003e 83.3 kDa (as provided).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e The purity information is not available for VLPs proteins.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eRegion choice, expression system, and tag\/format can influence folding, post-translational modifications, and interaction behavior in downstream assays.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eVLPs is a viral protein target frequently used in serology and antibody discovery workflows, where defined antigens enable consistent comparisons across samples and studies.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigen design and domain selection to better capture neutralizing versus non-neutralizing antibody responses.\u003c\/li\u003e\n\u003cli\u003eHigh-throughput serology and antibody screening using standardized antigens and plate-based formats.\u003c\/li\u003e\n\u003cli\u003eIntegrating binding kinetics with epitope mapping to support variant-aware immunology studies.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eCoat plates with VLPs antigen for ELISA antibody titration (serum\/plasma).\u003c\/li\u003e\n\u003cli\u003eScreen anti-VLPs antibodies by indirect ELISA and immunoblot readouts.\u003c\/li\u003e\n\u003cli\u003eMap antigenic epitopes using VLPs fragments\/domains (in vitro binding assays).\u003c\/li\u003e\n\u003cli\u003eDevelop antigen-capture assays using VLPs as a standard (spike-in controls).\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpret results in the context of the biological system, assay format, and any known domain\/isoform constraints for the target.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigenic proteins may contain immunodominant regions; domain choice can affect assay readouts and cross-reactivity.\u003c\/li\u003e\n\u003cli\u003eInclude relevant negative controls (e.g., unrelated antigens) and dilution series to support interpretation of binding signals.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - PubMed search — NLM: https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=VLPs - Reactome pathway browser — Reactome: https:\/\/reactome.org\/ - InterPro protein family resource — EMBL-EBI: https:\/\/www.ebi.ac.uk\/interpro\/ --\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059255042413,"sku":"CSB-MP3838f4-1MG","price":1770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059352985965,"sku":"CSB-MP3838f4-100UG","price":334.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059353018733,"sku":"CSB-MP3838f4-20UG","price":134.0,"currency_code":"USD","in_stock":true}]},{"product_id":"virus-like-particles-vlps-isotype-control-bhp10515264","title":"Virus-Like Particles (VLPs) isotype control","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eVirus-Like Particles (VLPs) isotype control is a recombinant protein preparation derived from the listed source organism. It is commonly used as a defined reagent for assay development, binding studies, and analytical controls where consistent protein specifications are required.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell (may influence folding and post-translational modifications).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag\/format:\u003c\/strong\u003e Tag-Free; Lyophilized powder.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpected size:\u003c\/strong\u003e 56.1 kDa (as provided).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e The purity information is not available for VLPs proteins.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eRegion choice, expression system, and tag\/format can influence folding, post-translational modifications, and interaction behavior in downstream assays.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eVLPs is a viral protein target frequently used in serology and antibody discovery workflows, where defined antigens enable consistent comparisons across samples and studies.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigen design and domain selection to better capture neutralizing versus non-neutralizing antibody responses.\u003c\/li\u003e\n\u003cli\u003eHigh-throughput serology and antibody screening using standardized antigens and plate-based formats.\u003c\/li\u003e\n\u003cli\u003eIntegrating binding kinetics with epitope mapping to support variant-aware immunology studies.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eCoat plates with VLPs antigen for ELISA antibody titration (serum\/plasma).\u003c\/li\u003e\n\u003cli\u003eScreen anti-VLPs antibodies by indirect ELISA and immunoblot readouts.\u003c\/li\u003e\n\u003cli\u003eMap antigenic epitopes using VLPs fragments\/domains (in vitro binding assays).\u003c\/li\u003e\n\u003cli\u003eDevelop antigen-capture assays using VLPs as a standard (spike-in controls).\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpret results in the context of the biological system, assay format, and any known domain\/isoform constraints for the target.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigenic proteins may contain immunodominant regions; domain choice can affect assay readouts and cross-reactivity.\u003c\/li\u003e\n\u003cli\u003eInclude relevant negative controls (e.g., unrelated antigens) and dilution series to support interpretation of binding signals.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - PubMed search — NLM: https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=VLPs - Reactome pathway browser — Reactome: https:\/\/reactome.org\/ - InterPro protein family resource — EMBL-EBI: https:\/\/www.ebi.ac.uk\/interpro\/ --\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059283255661,"sku":"CSB-MP3838-C-1MG","price":1770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059414491501,"sku":"CSB-MP3838-C-100UG","price":334.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059414524269,"sku":"CSB-MP3838-C-20UG","price":134.0,"currency_code":"USD","in_stock":true}]},{"product_id":"virus-like-particles-vlps-isotype-control-bhp10516912","title":"Virus-Like Particles (VLPs) isotype control","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eThis product is a recombinant VLPs protein commonly used as a defined reagent for assay development, interaction studies, and cell-based functional experiments. \u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell — expression context can influence folding and post-translational features.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eConjugate\/format:\u003c\/strong\u003e C-terminal 10xHis-tagged — useful for platform-specific capture or detection workflows.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eVLPs is studied for its biological roles within relevant pathways and cellular contexts. Recombinant reagents enable controlled dosing and binding measurements independent of endogenous expression.\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eAntigen design for serology assay development and immunoprofiling across cohorts.\u003c\/li\u003e \u003cli\u003eEpitope-focused studies evaluating variant-dependent antigenicity and antibody binding.\u003c\/li\u003e \u003cli\u003eUse of recombinant antigens as benchmarks in neutralization and binding platforms.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eUse as a reagent for consistent dosing across in vitro assays\u003c\/li\u003e \u003cli\u003eGenerate standard curves or spike-in controls in buffer or sample matrix for plate assays\u003c\/li\u003e \u003cli\u003eUse VLPs as antigen control for serology assay development and immunoreactivity testing\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eConsider isoforms, processing, or post-translational modifications that may differ from endogenous protein across systems.\u003c\/li\u003e \u003cli\u003eFor tagged or labeled formats, confirm that the tag does not occlude binding sites relevant to your readout.\u003c\/li\u003e \u003cli\u003eUse appropriate negative\/positive controls and orthogonal assays when interpreting binding or activity differences.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProt Knowledgebase (UniProt): https:\/\/www.uniprot.org\/ - NCBI Gene (NIH\/NCBI): https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - NCBI Protein (NIH\/NCBI): https:\/\/www.ncbi.nlm.nih.gov\/protein\/ - Reactome Pathway Database: https:\/\/reactome.org\/ - KEGG Pathway Database: https:\/\/www.kegg.jp\/ - NCBI Virus (NIH\/NCBI): https:\/\/www.ncbi.nlm.nih.gov\/labs\/virus\/ - ICTV Virus Taxonomy: https:\/\/ictv.global\/ --\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059852730733,"sku":"CSB-MP3838d7-1MG","price":1770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059915219309,"sku":"CSB-MP3838d7-100UG","price":334.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059915252077,"sku":"CSB-MP3838d7-20UG","price":134.0,"currency_code":"USD","in_stock":true}]},{"product_id":"virus-like-particles-vlps-isotype-control-mcherry-fluorescent-bhp10516913","title":"Virus-Like Particles (VLPs) isotype control-mCherry Fluorescent","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eThis product is a recombinant VLPs protein commonly used as a defined reagent for assay development, interaction studies, and cell-based functional experiments. \u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell — expression context can influence folding and post-translational features.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eConjugate\/format:\u003c\/strong\u003e C-terminal mCherry-tagged — useful for platform-specific capture or detection workflows.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eVLPs is studied for its biological roles within relevant pathways and cellular contexts. Recombinant reagents enable controlled dosing and binding measurements independent of endogenous expression.\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eAntigen design for serology assay development and immunoprofiling across cohorts.\u003c\/li\u003e \u003cli\u003eEpitope-focused studies evaluating variant-dependent antigenicity and antibody binding.\u003c\/li\u003e \u003cli\u003eUse of recombinant antigens as benchmarks in neutralization and binding platforms.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eUse as a reagent for consistent dosing across in vitro assays\u003c\/li\u003e \u003cli\u003eGenerate standard curves or spike-in controls in buffer or sample matrix for plate assays\u003c\/li\u003e \u003cli\u003eUse VLPs as antigen control for serology assay development and immunoreactivity testing\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eConsider isoforms, processing, or post-translational modifications that may differ from endogenous protein across systems.\u003c\/li\u003e \u003cli\u003eFor tagged or labeled formats, confirm that the tag does not occlude binding sites relevant to your readout.\u003c\/li\u003e \u003cli\u003eUse appropriate negative\/positive controls and orthogonal assays when interpreting binding or activity differences.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProt Knowledgebase (UniProt): https:\/\/www.uniprot.org\/ - NCBI Gene (NIH\/NCBI): https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - NCBI Protein (NIH\/NCBI): https:\/\/www.ncbi.nlm.nih.gov\/protein\/ - Reactome Pathway Database: https:\/\/reactome.org\/ - KEGG Pathway Database: https:\/\/www.kegg.jp\/ - NCBI Virus (NIH\/NCBI): https:\/\/www.ncbi.nlm.nih.gov\/labs\/virus\/ - ICTV Virus Taxonomy: https:\/\/ictv.global\/ --\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059853123949,"sku":"CSB-MP3838l5-1MG","price":1770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059915874669,"sku":"CSB-MP3838l5-100UG","price":334.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059915907437,"sku":"CSB-MP3838l5-20UG","price":134.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-b-lymphocyte-antigen-cd20-ms4a1-vlps-active-bhp10509494","title":"Recombinant Human B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–297 (297 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 4TM. 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P11836. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (B-lymphocyte surface antigen B1) (Bp35) (Leukocyte surface antigen Leu-16) (Membrane-spanning 4-domains subfamily A member 1) (CD antigen CD20).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active) (P11836) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P11836\/entry\n- NCBI Gene search: MS4A1 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MS4A1%20Homo%20sapiens\n- PubMed search: MS4A1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MS4A1%20review\n- InterPro search: MS4A1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/MS4A1\/\n- Ensembl Gene Summary: MS4A1 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=MS4A1\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207327670637,"sku":"CSB-MP015007HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320596226413,"sku":"CSB-MP015007HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320596259181,"sku":"CSB-MP015007HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP015007HU-WB.jpg?v=1778623133"},{"product_id":"recombinant-human-cannabinoid-receptor-1-cnr1-vlps-active-bhp10509501","title":"Recombinant Human Cannabinoid receptor 1 (CNR1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human Cannabinoid receptor 1 (CNR1)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P21554. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Cannabinoid receptor 1 (CNR1)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (CB-R)(CB1)(CANN6).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Cannabinoid receptor 1 (CNR1)-VLPs (Active) (P21554) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P21554\/entry\n- NCBI Gene search: CNR1 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CNR1%20Homo%20sapiens\n- PubMed search: CNR1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CNR1%20review\n- InterPro search: CNR1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CNR1\/\n- Ensembl Gene Summary: CNR1 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=CNR1\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207327736173,"sku":"CSB-MP005678HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320596324717,"sku":"CSB-MP005678HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320596357485,"sku":"CSB-MP005678HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005678HU-WB.jpg?v=1778623134"},{"product_id":"recombinant-human-claudin-18-2-cldn18-2-vlps-active-bhp10509475","title":"Recombinant Human Claudin-18.2 (CLDN18.2)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human Claudin-18.2 (CLDN18.2)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–261 (261 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 4TM. 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P56856-2. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Claudin-18.2 (CLDN18.2)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: CLDN18.2.\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Claudin-18.2 (CLDN18.2)-VLPs (Active) (P56856-2) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P56856-2\/entry\n- NCBI Gene search: CLDN18.2 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN18.2%20Homo%20sapiens\n- PubMed search: CLDN18.2 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN18.2%20review\n- InterPro search: CLDN18.2 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CLDN18.2\/\n- Ensembl Gene Summary: CLDN18.2 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=CLDN18.2\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207327834477,"sku":"CSB-MP005498HU(A5)-1MG","price":4940.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595505517,"sku":"CSB-MP005498HU(A5)-100UG","price":930.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595538285,"sku":"CSB-MP005498HU(A5)-20UG","price":456.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-8-ccr8-vlps-active-bhp10509485","title":"Recombinant Human C-C chemokine receptor type 8 (CCR8)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human C-C chemokine receptor type 8 (CCR8)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–355 (355 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P51685. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman C-C chemokine receptor type 8 (CCR8)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (CC chemokine receptor CHEMR1) (CMKBRL2) (Chemokine receptor-like 1) (CKR-L1) (GPR-CY6) (GPRCY6) (TER1) (CDw198) (CKRL1) (CMKBR8) (CMKBRL2).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human C-C chemokine receptor type 8 (CCR8)-VLPs (Active) (P51685) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P51685\/entry\n- NCBI Gene search: CCR8 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR8%20Homo%20sapiens\n- PubMed search: CCR8 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR8%20review\n- InterPro search: CCR8 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CCR8\/\n- Ensembl Gene Summary: CCR8 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=CCR8\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207328031085,"sku":"CSB-MP004847HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595079533,"sku":"CSB-MP004847HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595112301,"sku":"CSB-MP004847HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-c5a-anaphylatoxin-chemotactic-receptor-1-c5ar1-vlps-active-bhp10509495","title":"Recombinant Human C5a anaphylatoxin chemotactic receptor 1 (C5AR1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human C5a anaphylatoxin chemotactic receptor 1 (C5AR1)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–350 (350 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P21730. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman C5a anaphylatoxin chemotactic receptor 1 (C5AR1)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (C5a anaphylatoxin chemotactic receptor)(C5a-R)(C5aR)(CD88).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human C5a anaphylatoxin chemotactic receptor 1 (C5AR1)-VLPs (Active) (P21730) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P21730\/entry\n- NCBI Gene search: C5AR1 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=C5AR1%20Homo%20sapiens\n- PubMed search: C5AR1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=C5AR1%20review\n- InterPro search: C5AR1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/C5AR1\/\n- Ensembl Gene Summary: C5AR1 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=C5AR1\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207328129389,"sku":"CSB-MP003996HU-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595308909,"sku":"CSB-MP003996HU-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595341677,"sku":"CSB-MP003996HU-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP003996HU-WB.jpg?v=1778623137"},{"product_id":"recombinant-human-somatostatin-receptor-type-2-sstr2-vlps-active-bhp10509499","title":"Recombinant Human Somatostatin receptor type 2 (SSTR2)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human Somatostatin receptor type 2 (SSTR2)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–369 (369 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P30874. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Somatostatin receptor type 2 (SSTR2)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: SSTR2; Somatostatin receptor type 2; SS-2-R; SS2-R; SS2R; SRIF-1.\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Somatostatin receptor type 2 (SSTR2)-VLPs (Active) (P30874) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P30874\/entry\n- NCBI Gene search: SSTR2 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=SSTR2%20Homo%20sapiens\n- PubMed search: SSTR2 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SSTR2%20review\n- InterPro search: SSTR2 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/SSTR2\/\n- Ensembl Gene Summary: SSTR2 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=SSTR2\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207328457069,"sku":"CSB-MP022725HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320597307757,"sku":"CSB-MP022725HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320597340525,"sku":"CSB-MP022725HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP022725HU-AC1.jpg?v=1778623131"},{"product_id":"recombinant-human-g-protein-coupled-receptor-family-c-group-5-member-d-gprc5d-vlps-active-bhp10509498","title":"Recombinant Human G-protein coupled receptor family C group 5 member D (GPRC5D)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human G-protein coupled receptor family C group 5 member D (GPRC5D)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–345 (345 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q9NZD1. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman G-protein coupled receptor family C group 5 member D (GPRC5D)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Available annotations suggest it gprc5d in mm cells makes this gene and its encoded surface protein as promising markers for monitoring the tumor load and hopefully also as targets for antimyeloma antibodies. pmid: 23510526 overexpression of g protein-coupled receptor 5d in the bone marrow is associated with poor prognosis in patients with multiple myeloma. pmid: 22591013. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (GPRC5D)(G-protein coupled receptor family C group 5 member D).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human G-protein coupled receptor family C group 5 member D (GPRC5D)-VLPs (Active) (Q9NZD1) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q9NZD1\/entry\n- NCBI Gene search: GPRC5D Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=GPRC5D%20Homo%20sapiens\n- PubMed search: GPRC5D review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=GPRC5D%20review\n- InterPro search: GPRC5D — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/GPRC5D\/\n- Ensembl Gene Summary: GPRC5D (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=GPRC5D\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207328620909,"sku":"CSB-MP882153HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595767661,"sku":"CSB-MP882153HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595800429,"sku":"CSB-MP882153HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP882153HU-WB.jpg?v=1778623133"},{"product_id":"recombinant-dog-b-lymphocyte-antigen-cd20-ms4a1-vlps-active-bhp10509505","title":"Recombinant Dog B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Dog B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active) derived from Canis lupus familiaris (Dog) (Canis familiaris). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–297 (297 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 4TM. 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 Canis lupus familiaris (Dog) (Canis familiaris). 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 Q3C2E2. 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\u003eDog B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active) is a membrane-associated protein from Canis lupus familiaris. Available annotations suggest it b-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. functions as a store-operated calcium (soc) channel component promoting calcium influx after activation by the b-cell receptor\/bcr. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (Membrane-spanning 4-domains subfamily A member 1)(CD antigen CD20).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Dog B-lymphocyte antigen CD20 (MS4A1)-VLPs (Active) (Q3C2E2) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q3C2E2\/entry\n- NCBI Gene search: MS4A1 Canis lupus familiaris — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MS4A1%20Canis%20lupus%20familiaris\n- PubMed search: MS4A1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MS4A1%20review\n- InterPro search: MS4A1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/MS4A1\/\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207328751981,"sku":"CSB-MP661636DO-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595669357,"sku":"CSB-MP661636DO-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595702125,"sku":"CSB-MP661636DO-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP661636DO-WB.jpg?v=1778623133"},{"product_id":"recombinant-human-claudin-6-cldn6-vlps-active-bhp10509502","title":"Recombinant Human Claudin-6 (CLDN6)-VLPs (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 (Skullin)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003ePlays a major role in tight junction-specific obliteration of the intercellular space.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CLDN6 (also reported as (Skullin)). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-220aa. 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 95% as determined by SEC-HPLC.; molecular weight: 24.8 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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":53207329046893,"sku":"CSB-MP005508HU(A4)-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320597373293,"sku":"CSB-MP005508HU(A4)-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320597406061,"sku":"CSB-MP005508HU(A4)-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005508HU_A4_-WB.jpg?v=1778623135"},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-4-ccr4-vlps-active-bhp10509496","title":"Recombinant Human C-C chemokine receptor type 4 (CCR4)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human C-C chemokine receptor type 4 (CCR4)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–360 (360 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P51679. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman C-C chemokine receptor type 4 (CCR4)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: K5-5 CD_antigen: CD194.\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human C-C chemokine receptor type 4 (CCR4)-VLPs (Active) (P51679) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P51679\/entry\n- NCBI Gene search: CCR4 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR4%20Homo%20sapiens\n- PubMed search: CCR4 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR4%20review\n- InterPro search: CCR4 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CCR4\/\n- Ensembl Gene Summary: CCR4 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=CCR4\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207329079661,"sku":"CSB-MP004843HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595997037,"sku":"CSB-MP004843HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320596029805,"sku":"CSB-MP004843HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP004843HU-WB.jpg?v=1778623135"},{"product_id":"recombinant-macaca-fascicularis-claudin-18-2-cldn18-2-vlps-active-bhp10509500","title":"Recombinant Macaca fascicularis Claudin 18.2 (CLDN18.2)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Macaca fascicularis Claudin 18.2 (CLDN18.2)-VLPs (Active) derived from Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–261 (261 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 3TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). 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 A0A2K5VV62. 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\u003eMacaca fascicularis Claudin 18.2 (CLDN18.2)-VLPs (Active) is a membrane-associated protein from Macaca fascicularis. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: Claudin.\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Macaca fascicularis Claudin 18.2 (CLDN18.2)-VLPs (Active) (A0A2K5VV62) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/A0A2K5VV62\/entry\n- NCBI Gene search: CLDN18.2 Macaca fascicularis — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN18.2%20Macaca%20fascicularis\n- PubMed search: CLDN18.2 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN18.2%20review\n- InterPro search: CLDN18.2 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CLDN18.2\/\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207329112429,"sku":"CSB-MP4304MOV-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595374445,"sku":"CSB-MP4304MOV-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595407213,"sku":"CSB-MP4304MOV-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP4304MOV-WB.jpg?v=1778623131"},{"product_id":"recombinant-human-claudin-9-cldn9-vlps-active-bhp10509503","title":"Recombinant Human Claudin-9 (CLDN9)-VLPs (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)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003e\"Claudin association with CD81 defines hepatitis C virus entry.\" Harris H.J., Davis C., Mullins J.G., Hu K., Goodall M., Farquhar M.J., Mee C.J., McCaffrey K., Young S., Drummer H., Balfe P., McKeating J.A.\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)). 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 1-217aa. 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: Lyophilized powder; purity: The purity information is not available for VLPs proteins.; molecular weight: 24.2 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\u003eCLDN9 has been annotated as Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.; (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) entry into hepatic cells.. 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":53207329276269,"sku":"CSB-MP005511HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320596390253,"sku":"CSB-MP005511HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320596423021,"sku":"CSB-MP005511HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005511HU-WB.jpg?v=1778623133"},{"product_id":"recombinant-mouse-claudin-18-2-cldn18-2-vlps-active-bhp10509504","title":"Recombinant Mouse Claudin-18.2 (Cldn18.2)-VLPs (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 (Claudin-18)) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003e\"Claudin 18 is a novel negative regulator of bone resorption and osteoclast differentiation.\" Linares G.R., Brommage R., Powell D.R., Xing W., Chen S.T., Alshbool F.Z., Lau K.H., Wergedal J.E., Mohan S.\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 (Claudin-18)). 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 1-264aa of Isoform A2.1. 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: The purity information is not available for VLPs proteins.; 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 has been annotated as Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. 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":53207329538413,"sku":"CSB-MP005498MO(F3)-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320595931501,"sku":"CSB-MP005498MO(F3)-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595964269,"sku":"CSB-MP005498MO(F3)-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005498MO_F3_-WB.jpg?v=1778623134"},{"product_id":"recombinant-human-claudin-4-cldn4-vlps-active-bhp10510509","title":"Recombinant Human Claudin-4 (CLDN4)-VLPs (Active)","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: Lyophilized powder; purity: The purity information is not available for VLPs proteins.; molecular weight: 23.4 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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":53207330488685,"sku":"CSB-MP005506HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320598716781,"sku":"CSB-MP005506HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320598749549,"sku":"CSB-MP005506HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005506HU-WB.jpg?v=1778623135"},{"product_id":"recombinant-human-prominin-1-prom1-vlps-active-bhp10510921","title":"Recombinant Human Prominin-1 (PROM1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003ePROM1\u003c\/strong\u003e (also reported as Prominin-1 (Antigen AC133)(Prominin-like protein 1)(CD antigen CD133)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eMay play a role in cell differentiation, proliferation and apoptosis.\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 PROM1 (also reported as Prominin-1 (Antigen AC133)(Prominin-like protein 1)(CD antigen CD133)). 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 20-865aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 96.7 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\u003ePROM1 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: PROM1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=PROM1\n- NCBI Gene search: PROM1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=PROM1\n- Ensembl search: PROM1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=PROM1\n- AlphaFold DB search: PROM1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/PROM1\n- RCSB PDB search: PROM1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=PROM1\n- PubMed search: PROM1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=PROM1+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":53207331635565,"sku":"CSB-MP018751HU(A4)-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320601272685,"sku":"CSB-MP018751HU(A4)-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320601305453,"sku":"CSB-MP018751HU(A4)-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP018751HU_A4_-WB.jpg?v=1778623142"},{"product_id":"recombinant-human-kita-kyushu-lung-cancer-antigen-1-ct83-vlps-bhp10510927","title":"Recombinant Human Kita-kyushu lung cancer antigen 1 (CT83)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human Kita-kyushu lung cancer antigen 1 (CT83)-VLPs derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–113 (113 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 1TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt Q5H943. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Kita-kyushu lung cancer antigen 1 (CT83)-VLPs is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (KK-LC-1)(Cancer\/testis antigen 83).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Kita-kyushu lung cancer antigen 1 (CT83)-VLPs (Q5H943) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q5H943\/entry\n- NCBI Gene search: CT83 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CT83%20Homo%20sapiens\n- PubMed search: CT83 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CT83%20review\n- InterPro search: CT83 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CT83\/\n- Ensembl Gene Summary: CT83 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=CT83\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207331930477,"sku":"CSB-MP711093HU-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320601338221,"sku":"CSB-MP711093HU-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320601370989,"sku":"CSB-MP711093HU-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP711093HU-WB.jpg?v=1778623142"},{"product_id":"recombinant-human-umor-necrosis-factor-receptor-superfamily-member-16-ngfr-biotinylated-vlps-bhp10511845","title":"Recombinant Human umor necrosis factor receptor superfamily member 16 (NGFR), Biotinylated-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eNGFR\u003c\/strong\u003e (also reported as (Gp80-LNGFR)(Low affinity neurotrophin receptor p75NTR)(Low-affinity nerve growth factor receptor)(NGF receptor)(p75 ICD)(CD antigen CD271)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eLow affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4.\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 NGFR (also reported as (Gp80-LNGFR)(Low affinity neurotrophin receptor p75NTR)(Low-affinity nerve growth factor receptor)(NGF receptor)(p75 ICD)(CD antigen CD271)). 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 29-427aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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: The purity information is not available for VLPs proteins.; molecular weight: 46.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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\u003eNGFR 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: NGFR — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=NGFR\n- NCBI Gene search: NGFR — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=NGFR\n- Ensembl search: NGFR — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=NGFR\n- AlphaFold DB search: NGFR — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/NGFR\n- RCSB PDB search: NGFR — RCSB PDB — https:\/\/www.rcsb.org\/search?query=NGFR\n- PubMed search: NGFR transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=NGFR+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":53207332225389,"sku":"CSB-MP015780HU(A4)-B-1MG","price":6242.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320602255725,"sku":"CSB-MP015780HU(A4)-B-100UG","price":1340.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602288493,"sku":"CSB-MP015780HU(A4)-B-20UG","price":770.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-pendrin-slc26a4-vlps-bhp10511848","title":"Recombinant Human Pendrin (SLC26A4)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eSLC26A4\u003c\/strong\u003e (also reported as (Sodium-independent chloride\/iodide transporter)(Solute carrier family 26 member 4)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eSodium-independent transporter of chloride and iodide.\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 SLC26A4 (also reported as (Sodium-independent chloride\/iodide transporter)(Solute carrier family 26 member 4)). 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 1-780aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 86.7 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\u003eSLC26A4 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: SLC26A4 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=SLC26A4\n- NCBI Gene search: SLC26A4 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=SLC26A4\n- Ensembl search: SLC26A4 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=SLC26A4\n- AlphaFold DB search: SLC26A4 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/SLC26A4\n- RCSB PDB search: SLC26A4 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=SLC26A4\n- PubMed search: SLC26A4 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SLC26A4+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":53207332323693,"sku":"CSB-MP021527HU(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320602943853,"sku":"CSB-MP021527HU(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602976621,"sku":"CSB-MP021527HU(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-alpha-2a-adrenergic-receptor-adra2a-vlps-bhp10511839","title":"Recombinant Human Alpha-2A adrenergic receptor (ADRA2A)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eADRA2A\u003c\/strong\u003e (also reported as (Alpha-2 adrenergic receptor subtype C10)(Alpha-2A adrenoreceptor)(Alpha-2A adrenoceptor)(Alpha-2AAR)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eAlpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.\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 ADRA2A (also reported as (Alpha-2 adrenergic receptor subtype C10)(Alpha-2A adrenoreceptor)(Alpha-2A adrenoceptor)(Alpha-2AAR)). 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 1-465aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 52.0 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\u003eADRA2A 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: ADRA2A — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ADRA2A\n- NCBI Gene search: ADRA2A — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ADRA2A\n- Ensembl search: ADRA2A — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ADRA2A\n- AlphaFold DB search: ADRA2A — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ADRA2A\n- RCSB PDB search: ADRA2A — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ADRA2A\n- PubMed search: ADRA2A transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ADRA2A+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":53207332290925,"sku":"CSB-MP001388HU-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320603107693,"sku":"CSB-MP001388HU-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320603140461,"sku":"CSB-MP001388HU-20UG","price":620.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-claudin-3-cldn3-vlps-active-bhp10511490","title":"Recombinant Human Claudin-3 (CLDN3)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCLDN3\u003c\/strong\u003e (also reported as (Clostridium perfringens enterotoxin receptor 2)(CPE-R 2; CPE-receptor 2)(Rat ventral prostate.1 protein homolog)(hRVP1)) 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 CLDN3 (also reported as (Clostridium perfringens enterotoxin receptor 2)(CPE-R 2; CPE-receptor 2)(Rat ventral prostate.1 protein homolog)(hRVP1)). 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 1-220aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 24.7 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\u003eCLDN3 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: CLDN3 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CLDN3\n- NCBI Gene search: CLDN3 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CLDN3\n- Ensembl search: CLDN3 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CLDN3\n- AlphaFold DB search: CLDN3 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CLDN3\n- RCSB PDB search: CLDN3 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CLDN3\n- PubMed search: CLDN3 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CLDN3+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":53207332454765,"sku":"CSB-MP005505HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320603533677,"sku":"CSB-MP005505HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320603566445,"sku":"CSB-MP005505HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005505HU-WB.jpg?v=1778623144"},{"product_id":"recombinant-human-claudin-6-cldn6-fluorescent-vlps-active-bhp10511818","title":"Recombinant Human Claudin-6 (CLDN6), Fluorescent-VLPs (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 1-220aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 50.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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":53207332520301,"sku":"CSB-MP005508HU(A4)f4-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320602747245,"sku":"CSB-MP005508HU(A4)f4-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602780013,"sku":"CSB-MP005508HU(A4)f4-20UG","price":558.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-histamine-h3-receptor-hrh3-vlps-bhp10511855","title":"Recombinant Human Histamine H3 receptor (HRH3)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHRH3\u003c\/strong\u003e (also reported as (H3R)(HH3R)(G-protein coupled receptor 97)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eThe H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e HRH3 (also reported as (H3R)(HH3R)(G-protein coupled receptor 97)). 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 1-445aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 50.0 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\u003eHRH3 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: HRH3 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HRH3\n- NCBI Gene search: HRH3 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HRH3\n- Ensembl search: HRH3 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HRH3\n- AlphaFold DB search: HRH3 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HRH3\n- RCSB PDB search: HRH3 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HRH3\n- PubMed search: HRH3 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HRH3+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":53207332487533,"sku":"CSB-MP897568HU-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320602812781,"sku":"CSB-MP897568HU-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602845549,"sku":"CSB-MP897568HU-20UG","price":620.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-claudin-18-2-cldn18-2-fluorescent-vlps-active-bhp10511840","title":"Recombinant Human Claudin-18.2 (CLDN18.2), Fluorescent-VLPs (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: Lyophilized powder; purity: The purity information is not available for VLPs proteins.; molecular weight: 52.3 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\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":53207332651373,"sku":"CSB-MP005498HU(A5)l5-1MG","price":4940.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320601993581,"sku":"CSB-MP005498HU(A5)l5-100UG","price":930.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602026349,"sku":"CSB-MP005498HU(A5)l5-20UG","price":456.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-macaca-fascicularis-membrane-spanning-4-domains-a1-ms4a1-vlps-active-bhp10511492","title":"Recombinant Macaca fascicularis Membrane spanning 4-domains A1 (MS4A1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Macaca fascicularis Membrane spanning 4-domains A1 (MS4A1)-VLPs (Active) derived from Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–297 (297 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 4TM. 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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). 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 M4ZHZ6. 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\u003eMacaca fascicularis Membrane spanning 4-domains A1 (MS4A1)-VLPs (Active) is a membrane-associated protein from Macaca fascicularis. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: (Membrane spanning 4-domains A1)(Membrane-spanning 4-domains subfamily A member 1).\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Macaca fascicularis Membrane spanning 4-domains A1 (MS4A1)-VLPs (Active) (M4ZHZ6) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/M4ZHZ6\/entry\n- NCBI Gene search: MS4A1 Macaca fascicularis — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MS4A1%20Macaca%20fascicularis\n- PubMed search: MS4A1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MS4A1%20review\n- InterPro search: MS4A1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/MS4A1\/\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207332716909,"sku":"CSB-MP4516MOV-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320603042157,"sku":"CSB-MP4516MOV-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320603074925,"sku":"CSB-MP4516MOV-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP4516MOV-WB.jpg?v=1778623149"},{"product_id":"recombinant-human-prostatic-acid-phosphatase-acp3-vlps-bhp10511811","title":"Recombinant Human Prostatic acid phosphatase (ACP3)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eACP3\u003c\/strong\u003e (also reported as (PAP)(5'-nucleotidase)(5'-NT)(Acid phosphatase 3)(Ecto-5'-nucleotidase)(Protein tyrosine phosphatase ACP3)(Thiamine monophosphatase)(TMPase)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eA non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins .\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 ACP3 (also reported as (PAP)(5'-nucleotidase)(5'-NT)(Acid phosphatase 3)(Ecto-5'-nucleotidase)(Protein tyrosine phosphatase ACP3)(Thiamine monophosphatase)(TMPase)). 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 33-418aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 47.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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\u003eACP3 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: ACP3 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=ACP3\n- NCBI Gene search: ACP3 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=ACP3\n- Ensembl search: ACP3 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=ACP3\n- AlphaFold DB search: ACP3 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/ACP3\n- RCSB PDB search: ACP3 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=ACP3\n- PubMed search: ACP3 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=ACP3+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":53207332749677,"sku":"CSB-MP001181HU(F2)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320601928045,"sku":"CSB-MP001181HU(F2)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320601960813,"sku":"CSB-MP001181HU(F2)-20UG","price":620.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-mouse-melanocyte-stimulating-hormone-receptor-mc1r-vlps-bhp10511844","title":"Recombinant Mouse Melanocyte-stimulating hormone receptor (Mc1r)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMc1r\u003c\/strong\u003e (also reported as (MSH-R)(Melanocortin receptor 1)(MC1-R)) from Mus musculus (Mouse). In the supplied product notes, the target is described as \u003cem\u003eReceptor for MSH (alpha, beta and gamma) and ACTH.\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 Mc1r (also reported as (MSH-R)(Melanocortin receptor 1)(MC1-R)). 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 1-315aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 36.6 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\u003eMc1r 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: Mc1r — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=Mc1r\n- NCBI Gene search: Mc1r — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Mc1r\n- Ensembl search: Mc1r — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=Mc1r\n- AlphaFold DB search: Mc1r — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/Mc1r\n- RCSB PDB search: Mc1r — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Mc1r\n- PubMed search: Mc1r transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Mc1r+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":53207332782445,"sku":"CSB-MP013558MO-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320602124653,"sku":"CSB-MP013558MO-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602157421,"sku":"CSB-MP013558MO-20UG","price":620.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-histamine-h3-receptor-hrh3-fluorescent-vlps-bhp10511856","title":"Recombinant Human Histamine H3 receptor (HRH3), Fluorescent-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHRH3\u003c\/strong\u003e (also reported as (H3R)(HH3R)(G-protein coupled receptor 97)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eThe H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e HRH3 (also reported as (H3R)(HH3R)(G-protein coupled receptor 97)). 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 1-445aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 75.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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\u003eHRH3 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: HRH3 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HRH3\n- NCBI Gene search: HRH3 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HRH3\n- Ensembl search: HRH3 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HRH3\n- AlphaFold DB search: HRH3 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HRH3\n- RCSB PDB search: HRH3 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HRH3\n- PubMed search: HRH3 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HRH3+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":53207333437805,"sku":"CSB-MP897568HUf4-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320602452333,"sku":"CSB-MP897568HUf4-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320602485101,"sku":"CSB-MP897568HUf4-20UG","price":620.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-transmembrane-4-l6-family-member-1-tm4sf1-vlps-active-bhp10512397","title":"Recombinant Human Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active) derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–202 (202 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 4TM. 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P30408. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active) is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation. Also reported as: M3S1;TAAL6.\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active) (P30408) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P30408\/entry\n- NCBI Gene search: TM4SF1 Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=TM4SF1%20Homo%20sapiens\n- PubMed search: TM4SF1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=TM4SF1%20review\n- InterPro search: TM4SF1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/TM4SF1\/\n- Ensembl Gene Summary: TM4SF1 (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=TM4SF1\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207333732717,"sku":"CSB-MP023615HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605892973,"sku":"CSB-MP023615HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605925741,"sku":"CSB-MP023615HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP023615HU-WB.jpg?v=1778623150"},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-6-ccr6-vlps-active-bhp10512396","title":"Recombinant Human C-C chemokine receptor type 6 (CCR6)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCCR6\u003c\/strong\u003e (also reported as CKRL3;CMKBR6;GPR29;STRL22) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eAct as a receptor for the C-C type chemokine CCL20.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e CCR6 (also reported as CKRL3;CMKBR6;GPR29;STRL22). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-374aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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: The purity information is not available for VLPs proteins.; molecular weight: 42.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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\u003eCCR6 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: CCR6 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CCR6\n- NCBI Gene search: CCR6 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR6\n- Ensembl search: CCR6 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CCR6\n- AlphaFold DB search: CCR6 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CCR6\n- RCSB PDB search: CCR6 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CCR6\n- PubMed search: CCR6 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR6+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207333929325,"sku":"CSB-MP004845HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320604221805,"sku":"CSB-MP004845HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320604254573,"sku":"CSB-MP004845HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP004845HU-WB.jpg?v=1778623152"},{"product_id":"recombinant-macaca-fascicularis-transmembrane-4-l6-family-member-1-tm4sf1-vlps-active-bhp10512400","title":"Recombinant Macaca fascicularis Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Macaca fascicularis Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active) derived from Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 1–202 (202 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 4TM. 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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). 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 A0A2K5VKY2. 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\u003eMacaca fascicularis Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active) is a membrane-associated protein from Macaca fascicularis. 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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Macaca fascicularis Transmembrane 4 L6 family member 1 (TM4SF1)-VLPs (Active) (A0A2K5VKY2) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/A0A2K5VKY2\/entry\n- NCBI Gene search: TM4SF1 Macaca fascicularis — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=TM4SF1%20Macaca%20fascicularis\n- PubMed search: TM4SF1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=TM4SF1%20review\n- InterPro search: TM4SF1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/TM4SF1\/\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207334093165,"sku":"CSB-MP5031MOV-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320604647789,"sku":"CSB-MP5031MOV-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320604680557,"sku":"CSB-MP5031MOV-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP5031MOV-WB.jpg?v=1778623151"},{"product_id":"recombinant-human-type-2-angiotensin-ii-receptor-agtr2-vlps-bhp10512388","title":"Recombinant Human Type-2 angiotensin II receptor (AGTR2)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eAGTR2\u003c\/strong\u003e (also reported as (Angiotensin II type-2 receptor)(AT2 receptor)) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for angiotensin II, a vasoconstricting peptide.\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 AGTR2 (also reported as (Angiotensin II type-2 receptor)(AT2 receptor)). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-363aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 42.6 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\u003eAGTR2 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: AGTR2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=AGTR2\n- NCBI Gene search: AGTR2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=AGTR2\n- Ensembl search: AGTR2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=AGTR2\n- AlphaFold DB search: AGTR2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/AGTR2\n- RCSB PDB search: AGTR2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=AGTR2\n- PubMed search: AGTR2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=AGTR2+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":53207334257005,"sku":"CSB-MP001466HU(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320604877165,"sku":"CSB-MP001466HU(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320604909933,"sku":"CSB-MP001466HU(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP001466HU_A4_-WB.jpg?v=1778623221"},{"product_id":"recombinant-human-claudin-1-cldn1-vlps-active-bhp10512445","title":"Recombinant Human Claudin-1 (CLDN1)-VLPs (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 Claudin-1; 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 Claudin-1; 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 1-211aa. 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 95% as determined by SEC-HPLC.; molecular weight: 24.1 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":53207334617453,"sku":"CSB-MP005490HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320606187885,"sku":"CSB-MP005490HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320606220653,"sku":"CSB-MP005490HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP005490HU-WB.jpg?v=1778623153"},{"product_id":"recombinant-arabidopsis-thaliana-protein-hapless-2-hap2-vlps-bhp10512426","title":"Recombinant Arabidopsis thaliana Protein HAPLESS 2 (HAP2)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHAP2\u003c\/strong\u003e (also reported as GENERATIVE CELL SPECIFIC 1) from Arabidopsis thaliana (Mouse-ear cress). In the supplied product notes, the target is described as \u003cem\u003eRequired for male fertility.\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 HAP2 (also reported as GENERATIVE CELL SPECIFIC 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 25-705aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 80.3 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\u003eHAP2 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: HAP2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HAP2\n- NCBI Gene search: HAP2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HAP2\n- Ensembl search: HAP2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HAP2\n- AlphaFold DB search: HAP2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HAP2\n- RCSB PDB search: HAP2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HAP2\n- PubMed search: HAP2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HAP2+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":53207334715757,"sku":"CSB-MP518991DOA(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320606056813,"sku":"CSB-MP518991DOA(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320606089581,"sku":"CSB-MP518991DOA(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP518991DOA_A4_-WB.jpg?v=1778623159"},{"product_id":"recombinant-human-large-neutral-amino-acids-transporter-small-subunit-1-slc7a5-vlps-bhp10512440","title":"Recombinant Human Large neutral amino acids transporter small subunit 1 (SLC7A5)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eSLC7A5\u003c\/strong\u003e (also reported as 4F2 light chain;4F2 LC;4F2LC;CD98 light chain;Integral membrane protein E16;E16;L-type amino acid transporter 1;hLAT1;Solute carrier family 7 member 5;y+ system cationic amino acid transporter) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eThe heterodimer with SLC3A2 functions as sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, L-DOPA, leucine, histidine, methionine and tryptop…\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 SLC7A5 (also reported as 4F2 light chain;4F2 LC;4F2LC;CD98 light chain;Integral membrane protein E16;E16;L-type amino acid transporter 1;hLAT1;Solute carrier family 7 member 5;y+ system cationic amino acid transporter). 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 1-507aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 56.4 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\u003eSLC7A5 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: SLC7A5 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=SLC7A5\n- NCBI Gene search: SLC7A5 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=SLC7A5\n- Ensembl search: SLC7A5 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=SLC7A5\n- AlphaFold DB search: SLC7A5 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/SLC7A5\n- RCSB PDB search: SLC7A5 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=SLC7A5\n- PubMed search: SLC7A5 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SLC7A5+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":53207334781293,"sku":"CSB-MP021717HU(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605368685,"sku":"CSB-MP021717HU(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605401453,"sku":"CSB-MP021717HU(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP021717HU_A4_-WB.jpg?v=1778623152"},{"product_id":"recombinant-mouse-b-lymphocyte-antigen-cd20-ms4a1-vlps-bhp10512444","title":"Recombinant Mouse B-lymphocyte antigen CD20 (Ms4a1)-VLPs","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-cell differentiation antigen Ly-44;Lymphocyte antigen 44;Membrane-spanning 4-domains subfamily A member 1;CD antigen CD20) from Mus musculus (Mouse). 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.\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-cell differentiation antigen Ly-44;Lymphocyte antigen 44;Membrane-spanning 4-domains subfamily A member 1;CD antigen 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 1-291aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 33.7 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\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":53207335338349,"sku":"CSB-MP015007MO-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605041005,"sku":"CSB-MP015007MO-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605073773,"sku":"CSB-MP015007MO-20UG","price":558.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP015007MO-WB.jpg?v=1778623154"},{"product_id":"recombinant-rat-membrane-spanning-4-domains-a1-ms4a1-vlps-bhp10512443","title":"Recombinant Rat Membrane spanning 4-domains A1 (Ms4a1)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Rat Membrane spanning 4-domains A1 (Ms4a1)-VLPs derived from Rattus norvegicus (Rat). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–298 (298 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 4TM. 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 Rattus norvegicus (Rat). 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 D4A4Y3. 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\u003eRat Membrane spanning 4-domains A1 (Ms4a1)-VLPs is a membrane-associated protein from Rattus norvegicus. 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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Rat Membrane spanning 4-domains A1 (Ms4a1)-VLPs (D4A4Y3) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/D4A4Y3\/entry\n- NCBI Gene search: Ms4a1 Rattus norvegicus — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Ms4a1%20Rattus%20norvegicus\n- PubMed search: Ms4a1 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Ms4a1%20review\n- InterPro search: Ms4a1 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/Ms4a1\/\n- Ensembl Gene Summary: Ms4a1 (Rattus_norvegicus) — Ensembl — https:\/\/www.ensembl.org\/Rattus_norvegicus\/Gene\/Summary?g=Ms4a1\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207334945133,"sku":"CSB-MP5193RA-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605270381,"sku":"CSB-MP5193RA-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605303149,"sku":"CSB-MP5193RA-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP5193RA-WB.jpg?v=1778623150"},{"product_id":"recombinant-human-hla-drb1-and-hla-dra-heterodimer-protein-vlps-bhp10512421","title":"Recombinant Human HLA-DRB1\u0026HLA-DRA Heterodimer Protein-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Human HLA-DRB1\u0026amp;HLA-DRA Heterodimer Protein-VLPs derived from Homo sapiens (Human). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 30–266 (237 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 2TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Homo sapiens (Human). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt D7RIG5\u0026amp;P01903. Curated annotations and sequence features in public databases can help interpret domains, motifs, and known isoforms.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eMembrane proteins can be challenging analytes because conformation and interactions depend on the surrounding membrane environment. When using a recombinant region rather than a native membrane preparation, interpret binding and activity-oriented data in light of the construct boundaries, predicted topology, and expression host.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eHuman HLA-DRB1\u0026amp;HLA-DRA Heterodimer Protein-VLPs is a membrane-associated protein from Homo sapiens. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation.\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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Human HLA-DRB1\u0026HLA-DRA Heterodimer Protein-VLPs (D7RIG5\u0026P01903) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/D7RIG5%26P01903\/entry\n- NCBI Gene search: HLA-DRB1\u0026HLA-DRA Homo sapiens — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HLA-DRB1%26HLA-DRA%20Homo%20sapiens\n- PubMed search: HLA-DRB1\u0026HLA-DRA review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HLA-DRB1%26HLA-DRA%20review\n- InterPro search: HLA-DRB1\u0026HLA-DRA — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/HLA-DRB1%26HLA-DRA\/\n- Ensembl Gene Summary: HLA-DRB1\u0026HLA-DRA (Homo_sapiens) — Ensembl — https:\/\/www.ensembl.org\/Homo_sapiens\/Gene\/Summary?g=HLA-DRB1%26HLA-DRA\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207335076205,"sku":"CSB-MP5177HU-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605761901,"sku":"CSB-MP5177HU-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605794669,"sku":"CSB-MP5177HU-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP5177HU-WB.jpg?v=1778623155"},{"product_id":"recombinant-human-transient-receptor-potential-cation-channel-subfamily-m-member-8-trpm8-partial-vlps-bhp10512620","title":"Recombinant Human Transient receptor potential cation channel subfamily M member 8 (TRPM8), partial-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eTRPM8\u003c\/strong\u003e (also reported as Long transient receptor potential channel 6;LTrpC-6;LTrpC6;Transient receptor potential p8;Trp-p8) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius.\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 TRPM8 (also reported as Long transient receptor potential channel 6;LTrpC-6;LTrpC6;Transient receptor potential p8;Trp-p8). 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 690-1104aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 50.5 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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\u003eTRPM8 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: TRPM8 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=TRPM8\n- NCBI Gene search: TRPM8 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=TRPM8\n- Ensembl search: TRPM8 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=TRPM8\n- AlphaFold DB search: TRPM8 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/TRPM8\n- RCSB PDB search: TRPM8 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=TRPM8\n- PubMed search: TRPM8 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=TRPM8+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":53207335043437,"sku":"CSB-MP768757HU1-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320606679405,"sku":"CSB-MP768757HU1-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320606712173,"sku":"CSB-MP768757HU1-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP768757HU1-WB.jpg?v=1778623157"},{"product_id":"recombinant-macaca-fascicularis-chemokine-receptor-8-ccr8-vlps-bhp10512622","title":"Recombinant Macaca fascicularis Chemokine receptor 8 (CCR8)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product consists of virus-like particles (VLPs) displaying Macaca fascicularis Chemokine receptor 8 (CCR8)-VLPs derived from Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). VLP-based presentation can help maintain membrane topology and conformational epitopes for multi-pass proteins, supporting reagent development and binding-focused research. 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 1–355 (355 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 7TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). 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 G7NYJ2. 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\u003eMacaca fascicularis Chemokine receptor 8 (CCR8)-VLPs is a membrane-associated protein from Macaca fascicularis. 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\u003eVLP display considerations:\u003c\/strong\u003e VLP-based presentation can enrich for native-like membrane topology, but accessibility of specific loops\/epitopes can still vary with particle composition and protein orientation. Interpreting binding data benefits from using multiple controls and orthogonal readouts.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Macaca fascicularis Chemokine receptor 8 (CCR8)-VLPs (G7NYJ2) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/G7NYJ2\/entry\n- NCBI Gene search: CCR8 Macaca fascicularis — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR8%20Macaca%20fascicularis\n- PubMed search: CCR8 review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR8%20review\n- InterPro search: CCR8 — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/CCR8\/\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- PubMed search: virus-like particles membrane protein display review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=virus-like%20particles%20membrane%20protein%20display%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207335141741,"sku":"CSB-MP2709MOV-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320606581101,"sku":"CSB-MP2709MOV-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320606613869,"sku":"CSB-MP2709MOV-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP2709MOV-WB.jpg?v=1778623155"},{"product_id":"recombinant-crimean-congo-hemorrhagic-fever-virus-envelopment-polyprotein-gp-partial-vlps-bhp10512597","title":"Recombinant Crimean-Congo hemorrhagic fever virus Envelopment polyprotein (GP), partial-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eGP\u003c\/strong\u003e (also reported as M polyprotein;Gn;37 kDa protein;Glycoprotein G2;NSm;15 kDa protein;Gc;75 kDa protein;Glycoprotein G1) from Crimean-Congo hemorrhagic fever virus (strain Nigeria\/IbAr10200\/1970) (CCHFV). In the supplied product notes, the target is described as \u003cem\u003eGlycoprotein N]: Glycoprotein N and glycoprotein C interact with each other and are present at the surface of the virion (Probable).\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 GP (also reported as M polyprotein;Gn;37 kDa protein;Glycoprotein G2;NSm;15 kDa protein;Gc;75 kDa protein;Glycoprotein G1). 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 995-1684aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 79.3 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\u003eGP 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: GP — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=GP\n- NCBI Gene search: GP — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=GP\n- Ensembl search: GP — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=GP\n- AlphaFold DB search: GP — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/GP\n- RCSB PDB search: GP — RCSB PDB — https:\/\/www.rcsb.org\/search?query=GP\n- PubMed search: GP transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=GP+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":53207335174509,"sku":"CSB-MP810349CSC-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605663597,"sku":"CSB-MP810349CSC-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605696365,"sku":"CSB-MP810349CSC-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP810349CSC-WB.jpg?v=1778623154"},{"product_id":"recombinant-human-membrane-protein-mlc1-mlc1-vlps-bhp10512594","title":"Recombinant Human Membrane protein MLC1 (MLC1)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMLC1\u003c\/strong\u003e (also reported as MLC1) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eRegulates the response of astrocytes to hypo-osmosis by promoting calcium influx.\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 MLC1 (also reported as MLC1). 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 1-377aa. 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: The purity information is not available for VLPs proteins.; molecular weight: 42.6 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\u003eMLC1 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: MLC1 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=MLC1\n- NCBI Gene search: MLC1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MLC1\n- Ensembl search: MLC1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=MLC1\n- AlphaFold DB search: MLC1 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/MLC1\n- RCSB PDB search: MLC1 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=MLC1\n- PubMed search: MLC1 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MLC1+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":53207335108973,"sku":"CSB-MP613581HU(A5)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320605827437,"sku":"CSB-MP613581HU(A5)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320605860205,"sku":"CSB-MP613581HU(A5)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP613581HU_A5_-WB.jpg?v=1778623165"},{"product_id":"recombinant-macaca-mulatta-c-c-chemokine-receptor-type-8-ccr8-vlps-bhp10512621","title":"Recombinant Macaca mulatta C-C chemokine receptor type 8 (CCR8)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCCR8\u003c\/strong\u003e (also reported as C-C CKR-8;CC-CKR-8;CCR-8;CD antigen CDw198) from Macaca mulatta (Rhesus macaque). In the supplied product notes, the target is described as \u003cem\u003eReceptor for the chemokines CCL1\/SCYA1\/I-309.\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 CCR8 (also reported as C-C CKR-8;CC-CKR-8;CCR-8;CD antigen CDw198). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-356aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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: The purity information is not available for VLPs proteins.; molecular weight: 43.0 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\u003eCCR8 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: CCR8 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CCR8\n- NCBI Gene search: CCR8 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR8\n- Ensembl search: CCR8 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CCR8\n- AlphaFold DB search: CCR8 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CCR8\n- RCSB PDB search: CCR8 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CCR8\n- PubMed search: CCR8 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR8+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":53207335469421,"sku":"CSB-MP004847MOW-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320607039853,"sku":"CSB-MP004847MOW-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320607072621,"sku":"CSB-MP004847MOW-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP004847MOW-WB.jpg?v=1778623152"},{"product_id":"recombinant-human-myelin-oligodendrocyte-glycoprotein-mog-fluorescent-vlps-bhp10512854","title":"Recombinant Human Myelin-oligodendrocyte glycoprotein (MOG), Fluorescent-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMOG\u003c\/strong\u003e from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eMediates homophilic cell-cell adhesion.\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 MOG. 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 30-247aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e 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: The purity information is not available for VLPs proteins.; molecular weight: 55.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. 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\u003eMOG is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. 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: MOG — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=MOG\n- NCBI Gene search: MOG — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MOG\n- Ensembl search: MOG — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=MOG\n- AlphaFold DB search: MOG — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/MOG\n- RCSB PDB search: MOG — RCSB PDB — https:\/\/www.rcsb.org\/search?query=MOG\n- PubMed search: MOG transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MOG+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":53207335633261,"sku":"CSB-MP619083HU(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320607105389,"sku":"CSB-MP619083HU(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320607138157,"sku":"CSB-MP619083HU(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP619083HU_A4_-WB.jpg?v=1778623157"},{"product_id":"recombinant-human-c-c-chemokine-receptor-type-9-ccr9-vlps-active-bhp10512167","title":"Recombinant Human C-C chemokine receptor type 9 (CCR9)-VLPs (Active)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eCCR9\u003c\/strong\u003e (also reported as C-C CKR-9; CC-CKR-9; CCR-9;G-protein coupled receptor 28;GPR-9-6) from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eReceptor for chemokine SCYA25\/TECK.\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 CCR9 (also reported as C-C CKR-9; CC-CKR-9; CCR-9;G-protein coupled receptor 28;GPR-9-6). 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: Lyophilized powder; purity: Greater than 95% as determined by SEC-HPLC.; molecular weight: 43.4 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\u003eCCR9 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: CCR9 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=CCR9\n- NCBI Gene search: CCR9 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=CCR9\n- Ensembl search: CCR9 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=CCR9\n- AlphaFold DB search: CCR9 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/CCR9\n- RCSB PDB search: CCR9 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=CCR9\n- PubMed search: CCR9 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=CCR9+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":53207335764333,"sku":"CSB-MP004848HU-1MG","price":5891.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320604320109,"sku":"CSB-MP004848HU-100UG","price":1112.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320604352877,"sku":"CSB-MP004848HU-20UG","price":558.0,"currency_code":"USD","in_stock":true}]}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/collections\/virus-like-particles.png?v=1780678158","url":"https:\/\/www.ebiohippo.com\/collections\/vlp-membrane-proteins.oembed?page=2","provider":"BioHippo","version":"1.0","type":"link"}