

| Catalog No. | VK449024 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Description |
Anti-HPV B19 VP1/Coat protein VP1 Polyclonal Antibody (VK449024) is a rabbit polyclonal antibody detecting VP1 in ELISA, IHC, WB.
Highlights
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| Species reactivity | Human parvovirus B19 | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Human parvovirus B19 (HPV B19) VP1/Coat protein VP1 (His80-Ser227). | ||||||||
| Target | capsid protein 1, VP1 | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | P07299, Q9PZT0 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Background | Minor capsid protein VP1 (Coat protein VP1) is a ~86 kDa protein. Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. | ||||||||
| Note | For research use only. |


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