Coronavirus Spike Glycoprotein, Recombinant, Bovine, aa326-540, His-Tag (S)
Catalog No : USB-372847
1281.00€
0.00€
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| Product name | Coronavirus Spike Glycoprotein, Recombinant, Bovine, aa326-540, His-Tag (S) | ||
|---|---|---|---|
| Catalog No | USB-372847 | ||
| Supplier’s Catalog No | 372847 | ||
| Supplier | US Biologicals | ||
| Source antigen | Recombinant, Yeast | ||
| Reactivity | |||
| Cross reactivity | None | ||
| Applications | User defined | ||
| Molecular weight | 25,7 KDa | ||
| Storage | -20°C | ||
|---|---|---|---|
| Other names | |||
| Grade | Highly Purified | ||
| Purity | ~90% (SDS-PAGE) | ||
| Form | Supplied as a liquid in Tris, 50% glycerol. | ||
| Reactivity life | 6 months | ||
| Note | For reserch purpose only | ||
| Purity | ~90% (SDS-PAGE) | ||
| Description | S1 attaches the virion to the cell membrane by binding to 9-O-acetylated sialic acid containing proteins, initiating the infection. S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Source: Recombinant protein corresponding to aa326-540 from bovine S, fused to His-Tag at N-terminal, expressed in Yeast. Molecular Weight: ~25.7kD AA Sequence: PNLPDCNIEAWLNDKSVPSPLNWERKTFSNCNFNMSSLMSFIQADSFTCNNIEAAKIYGMCFSSITIDKFAIPNGRKVDLQLGNLGYLQSFNYRIDTTAASCQLYYNLPAANVSVSRFNPSTWNRRFGFTEQSVFKPQPVGVFTHHDVVYAQHCFKAPTNFCPCKLDGSLCVGNGPGIDAGYKNSGIGTCPAGTNYLTCHNAAQCDCLCTPDPIT Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. | ||
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