

| Catalog No. | VK665012 |
|---|---|
| Description |
Recombinant HHV-5/HCMV glycoprotein H/gH, N-His (VK665012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | P12824 |
| Protein length | Phe298-Val605 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Human cytomegalovirus (HCMV) (HHV-5) (Human herpesvirus 5) |
| 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 | Envelope glycoprotein H, UL75, gH |
| Background | Envelope glycoprotein H is a ~84 kDa protein. The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. In human cytomegalovirus, forms two distinct complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA, and in glioblastoma cells by interacting with host EPHA2. |
| Note | For research use only |




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