{"product_id":"recombinant-measles-virus-fusion-glycoprotein-f0-f-bhp10508856","title":"Recombinant Measles virus Fusion glycoprotein F0 (F)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis product is a recombinant protein derived from Measles virus (strain Leningrad-16) (MeV) (Subacute sclerose panencephalitis virus): Measles virus Fusion glycoprotein F0 (F) corresponding to amino acids 24–550. Defined recombinant constructs are commonly used as antigens or biochemical tools for antibody generation, interaction studies, and assay development. This material is supplied for research use only (RUO).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e Amino acids 24–550 (527 aa) from the annotated sequence. Region choice can affect folding, solubility, and which epitopes are represented.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTransmembrane architecture:\u003c\/strong\u003e Annotated as 1TM. Predicted topology influences detergent\/lipid dependence, epitope accessibility (extracellular vs cytosolic loops), and how results translate to full-length proteins in membranes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Bacterial expression typically yields non-glycosylated protein and may require careful interpretation for eukaryotic membrane proteins where post-translational modifications can influence conformation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Measles virus (strain Leningrad-16) (MeV) (Subacute sclerose panencephalitis virus). Ortholog differences can affect epitope conservation and functional interpretation across model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReference accession:\u003c\/strong\u003e UniProt P69356. 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\u003eMeasles virus Fusion glycoprotein F0 (F) is a membrane-associated protein from Measles virus. Many membrane proteins participate in transport, signaling, cell–cell interactions, or host–pathogen processes. For less-characterized entries, curated database annotations (e.g., UniProt) and domain predictions provide useful starting points for hypothesis generation.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIntegrating domain prediction, topology mapping, and comparative genomics to refine functional hypotheses for membrane proteins.\u003c\/li\u003e\n\u003cli\u003eUsing structural and biophysical methods (including stabilized constructs and membrane mimetics) to probe conformation and interactions.\u003c\/li\u003e\n\u003cli\u003eApplying single-cell and spatial omics to understand when and where membrane proteins are expressed and how that links to phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eAntigen production for antibody generation, epitope mapping, or binder screening against defined regions.\u003c\/li\u003e\n\u003cli\u003eBiochemical interaction studies (protein–protein or protein–lipid) that inform pathway placement and mechanism.\u003c\/li\u003e\n\u003cli\u003eComparative studies of orthologs\/variants to explore conserved motifs and potential functional differences.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signals from binding or detection assays, changes may reflect altered abundance, localization, or accessibility of the targeted region rather than changes in intrinsic activity. Pairing recombinant-protein results with cellular context (e.g., overexpression\/knockdown comparisons or orthogonal readouts) can strengthen conclusions without relying on any single assay format.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli\u003eIsoforms, sequence variants, and proteolytic processing can change which extracellular or cytosolic regions are present and therefore which epitopes are detected.\u003c\/li\u003e\n\u003cli\u003ePost-translational modifications (e.g., glycosylation, disulfide bonding) and the membrane environment can influence conformation and binding; this can differ by expression system and sample type.\u003c\/li\u003e\n\u003cli\u003eUse appropriate negative\/positive control concepts (e.g., knockout\/knockdown or overexpression controls, orthogonal antibodies\/assays, and matched species\/ortholog controls) to support specificity.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eRecombinant protein considerations:\u003c\/strong\u003e Because E. coli does not perform most eukaryotic glycosylation and certain processing events, some epitopes or activities that depend on these features may not be fully represented. For many workflows (e.g., antibody generation or domain-focused binding studies), a well-defined region is still highly useful, especially when paired with orthogonal validation in cells or membranes.\u003c\/p\u003e\n\u003c!-- Sources (internal):\n- UniProtKB entry for Measles virus Fusion glycoprotein F0 (F) (P69356) — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P69356\/entry\n- NCBI Gene search: F Measles virus — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=F%20Measles%20virus\n- PubMed search: F review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=F%20review\n- InterPro search: F — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/F\/\n- InterPro topic search: transmembrane protein — EMBL-EBI — https:\/\/www.ebi.ac.uk\/interpro\/search\/text\/transmembrane%20protein\/\n- PubMed search: membrane protein expression in E. coli review — NIH\/NLM — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane%20protein%20expression%20E.%20coli%20review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207326982509,"sku":"CSB-CF300829MCX-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320594325869,"sku":"CSB-CF300829MCX-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF300829MCX-SDS.jpg?v=1778623128","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-measles-virus-fusion-glycoprotein-f0-f-bhp10508856","provider":"BioHippo","version":"1.0","type":"link"}