{"product_id":"recombinant-mumps-virus-fusion-glycoprotein-f0-f-partial-biotinylated-bhp10516122","title":"Recombinant Mumps virus Fusion glycoprotein F0 (F), partial, Biotinylated","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eRecombinant Mumps virus Fusion glycoprotein F0 (F), partial, Biotinylated is a recombinant protein preparation derived from Mumps virus (strain RW) (MuV). 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\u003eExpressed region:\u003c\/strong\u003e 20-486aa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli (may influence folding and post-translational modifications).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag\/format:\u003c\/strong\u003e N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged; Liquid or Lyophilized powder.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpected size:\u003c\/strong\u003e 98.6 kDa (as provided).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 85% as determined by SDS-PAGE.\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\u003eClass I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis\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 MuV-F antigen for ELISA antibody titration (serum\/plasma).\u003c\/li\u003e\n\u003cli\u003eScreen anti-MuV-F antibodies by indirect ELISA and immunoblot readouts.\u003c\/li\u003e\n\u003cli\u003eMap antigenic epitopes using MuV-F fragments\/domains (in vitro binding assays).\u003c\/li\u003e\n\u003cli\u003eDevelop antigen-capture assays using MuV-F 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): - UniProtKB entry (P09458) — UniProt: https:\/\/www.uniprot.org\/uniprotkb\/P09458 - NCBI Gene search (F) — NCBI: https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=F - PubMed search — NLM: https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MuV-F - Reactome pathway browser — Reactome: https:\/\/reactome.org\/ - InterPro protein family resource — EMBL-EBI: https:\/\/www.ebi.ac.uk\/interpro\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059308192109,"sku":"CSB-EP357683MJK1-B-1MG","price":2960.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059459023213,"sku":"CSB-EP357683MJK1-B-100UG","price":874.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059459055981,"sku":"CSB-EP357683MJK1-B-20UG","price":466.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP357683MJK1-B-SDS.jpg?v=1772280373","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-mumps-virus-fusion-glycoprotein-f0-f-partial-biotinylated-bhp10516122","provider":"BioHippo","version":"1.0","type":"link"}