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Anti-BKPyV VP1 Monoclonal Antibody
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Product Description:The Anti-BKPyV VP1 antibody is a human monoclonal antibody recommended for use in enzyme-linked immunosorbent assay and other applications. This antibody specifically targets BKPyV VP1 and demonstrates reactivity with BK Virus.Applications:Enzyme-Linked Immunosorbent AssaySource:HumanTarget:BKPyV VP1Target Species:BK VirusSpecificity:This antibody reacts with BKPyV VP1.Clonality:MonoclonalPurification:The antibody was purified by affinity chromatography.Purity:>95% as determined by SDS-PAGEAggregation:<5% as determined by SECConcentration:1 mg/mLForm:LiquidEndotoxin:Please contact us for more information.Formulation:Contact us for custom product formulation.Preservative:BSA and Azide free.Stabilizer:NoneShipping:Shipped at 4°C.Storage:This antibody can be stored at 2°C-8°C for one month. Upon delivery aliquot. For longer storage, store at -20°C. Avoid repeated freeze-thaw cycles.
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Anti-BKPyV VP1 Monoclonal Antibody Applications
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Note:Optimal dilutions/concentrations should be determined by the end user.
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Protein Name
Major capsid protein VP1
Introduction
VP1 is the major capsid protein of the BK polyomavirus (BKPyV), a common human virus that is usually asymptomatic but can cause severe complications, particularly nephropathy in immunocompromised individuals. VP1 is the primary structural component of the viral capsid and is essential for viral attachment to host cells.
Alternative Names
Major capsid protein VP1; Major structural protein VP1; Human polyomavirus 1; BK polyomavirus Major capsid protein VP1; BKPyV VP1
Gene ID
UniProt
Subcellular Location
Virion. Host nucleus
Function
Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
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