

| Catalog No. | VK666013 | ||||
|---|---|---|---|---|---|
| Description |
Anti-HCoV-229E Spike Protein Antibody (SAA2363) [SAA2363] (VK666013) is a human monoclonal antibody detecting Spike glycoprotein in ELISA, Neutralization. Suitable for HCoV-229E.
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| Species reactivity | HCoV-229E | ||||
| Applications | ELISA, Neutralization | ||||
| Host species | Human | ||||
| Isotype | IgG | ||||
| Clone ID | SAA2363 | ||||
| Clonality | Monoclonal | ||||
| Target | Spike glycoprotein, S glycoprotein, E2, Peplomer protein, S | ||||
| Endotoxin level | Please contact with the lab for this information. | ||||
| Purity | >95% as determined by SDS-PAGE. | ||||
| Purification | Protein A/G purified from cell culture supernatant. | ||||
| Accession | P15423 | ||||
| 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. |
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| Product Usage Information |
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| 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. | ||||
| Background | Spike glycoprotein is a ~128 kDa protein. S1 region attaches the virion to the cell membrane by interacting with host ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the 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) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. | ||||
| Note | For research use only |

SDS-PAGE for Anti-HCoV-229E Spike Protein Antibody (SAA2363)



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