

| Catalog No. | VK728022 |
|---|---|
| Description |
Recombinant RUBV Spike Glycoprotein E2, N-His (VK728022) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | Q8VA10 |
| Protein length | His376-Ser520 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Rubella virus (RUBV) |
| 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 | C, Capsid protein, Coat protein, E1 envelope glycoprotein, E2 envelope glycoprotein, Spike glycoprotein E1, Spike glycoprotein E2, Structural polyprotein, p110 |
| Background | Structural polyprotein is a ~114 kDa protein. Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. |
| Note | For research use only |


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