



| Catalog No. | VK698016 |
|---|---|
| Description |
Traxivitug (VK698016) is a research-grade recombinant antibody targeting Major capsid protein VP1. Produced in mammalian cells with native-like glycosylation.
Highlights
|
| Species reactivity | BK polyomavirus (BKPyV) |
| Applications | ELISA, Bioactivity: FACS, Functional assay, Research in vivo |
| Host species | Human |
| Isotype | IgG1-lambda2 |
| Expression system | Mammalian cells |
| Clonality | Monoclonal |
| Target | Major capsid protein VP1, Major structural protein VP1 |
| Endotoxin level | Please contact the lab for this information. |
| Purity | >95% purity as determined by SDS-PAGE. |
| Purification | Protein A/G purified from cell culture supernatant. |
| Accession | P03088 |
| Form | Liquid |
| Storage buffer | 0.01M PBS pH 7.4 Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| 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. |
| Alternate Names | 2770852-89-4, MAU868 |
| Background | Major capsid protein VP1 is a ~40 kDa protein. 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. |
| Note | For research use only. Not suitable for clinical or therapeutic use. |

SDS-PAGE for Research Grade Traxivitug.

Detects recombinant BKPyV VP1 (Catalog No: VK452011) in indirect ELISA.


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