{"product_id":"recombinant-rotavirus-a-outer-capsid-protein-vp4-partial-bhp10507432","title":"Recombinant Rotavirus A Outer capsid protein VP4, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eThis Recombinant Protein provides recombinant \u003cstrong\u003eVP4\u003c\/strong\u003e from Rotavirus A (strain RVA\/Human\/United States\/DS-1\/1976\/G2P1B[4]) (RV-A) (Rotavirus A (strain DS1)), produced in E.coli (region 247-479aa). It is commonly used as a defined reagent for assay development, binding studies, and mechanistic research (RUO).\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRegion:\u003c\/strong\u003e 247-479aa (domain boundaries can affect binding\/activity readouts).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression host:\u003c\/strong\u003e E.coli (may differ from native PTMs\/processing).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s):\u003c\/strong\u003e His, Myc (supports purification\/detection; consider tag effects in controls).\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eAlso reported as Hemagglutinin. Outer capsid protein VP4: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca2+ concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts.Outer capsid protein VP5*: Forms the spike \"foot\" and \"body\" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2\/ITGB1 for cell attachment.Outer capsid protein VP8*: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo-blood group antigens for viral entry.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\u003cli\u003eUse of recombinant standards to improve assay calibration and cross-study comparability.\u003c\/li\u003e\u003c\/ul\u003e\u003cp\u003eOuter capsid protein VP4: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca2+ concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts.Outer capsid protein VP5*: Forms the spike \"foot\" and \"body\" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2\/ITGB1 for cell attachment.Outer capsid protein VP8*: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo-blood group antigens for viral entry.\u003c\/p\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eStandard curve or spike-in reference for quantitative assays involving VP4\u003c\/li\u003e\n\u003cli\u003eBinding and specificity benchmarking for detection reagents (conceptual)\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eRecombinant constructs may not capture all native isoforms or PTMs.\u003c\/li\u003e\n\u003cli\u003eConsider tag- or host-related effects when interpreting binding or activity.\u003c\/li\u003e\n\u003cli\u003eUse appropriate blanks and matrix\/control concepts to separate signal from background.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProtKB P11196 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P11196 - NCBI Gene search: VP4 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=VP4 - Ensembl search: VP4 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=VP4 - Reactome Pathway Browser — Reactome — https:\/\/reactome.org\/ - NCBI Bookshelf — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/books\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53053413654893,"sku":"CSB-EP319263ROJ-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53053546529133,"sku":"CSB-EP319263ROJ-100UG","price":729.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53053546561901,"sku":"CSB-EP319263ROJ-20UG","price":388.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP319263ROJ-SDS.jpg?v=1772177672","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-rotavirus-a-outer-capsid-protein-vp4-partial-bhp10507432","provider":"BioHippo","version":"1.0","type":"link"}