

| Catalog No. | VK802012 |
|---|---|
| Description |
Recombinant HHAV Protease 3C Protein, N-His (VK802012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | A3FMB2 |
| Protein length | Ser1520-Gln1738 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Hepatitis A virus (HAV) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 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 | Assembly signal 2A, Capsid protein VP0, Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, Capsid protein VP4, EC:2.7.7.48, EC:3.4.22.28, EC:3.6.1.15, Genome polyprotein, P1A, P1B, P1C, P1D, P2B, P2C, P3, P3A, P3B, P3C, P3D-POL, Picornain 3C, Protease 3C, Protein 2B, Protein 2BC, Protein 2C, Protein 3A, Protein 3AB, Protein 3ABC, Protein 3ABCD, Protein 3B, Protein 3CD, Protein VP1-2A, RNA-directed RNA polymerase 3D-POL, VP4-VP2, VPX, VPg, Viral protein genome-linked, Virion protein 1, Virion protein 2, Virion protein 3, Virion protein 4, pX |
| Background | Genome polyprotein is a ~251 kDa protein. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. |
| Note | For research use only |
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