| Reactivity | VSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Additional Information | 5 Point Mutations (D614G, R682S, R685S, K986P, V987P) |
| Details of Functionality | Measured by its binding ability in a functional ELISA with Recombinant Human ACE-2 His-tag (Catalog #
933-ZN). |
| Source | Human embryonic kidney cell, HEK293-derived sars-cov-2 Spike protein Val16-Lys1211 (Asp614Gly, Arg682Ser, Arg685Ser, Lys986Pro, Val987Pro), with a C-terminal His-tag |
| Accession # | |
| N-terminal Sequence | Val16 |
| Protein/Peptide Type | Recombinant Proteins |
| Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 134 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| SDS-PAGE | 140-160 kDa, under reducing conditions. |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions | Reconstitute at 500 μg/mL in PBS. |
SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1). SARS-CoV-2 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2 (2). In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into the S1 and S2 subunits is required for activation. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (3-5). A SARS-CoV-2 variant carrying the S protein amino acid (aa) change D614G has become the most prevalent form in the global pandemic and has been associated with greater infectivity and higher viral load (6,7). The S protein of SARS-CoV-2 shares 75% and 29% aa sequence identity with S protein of SARS-CoV-1 and MERS, respectively. The S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds Angiotensin-Converting Enzyme 2 (ACE2), but with much higher affinity and faster binding kinetics through the receptor binding domain (RBD) located in the C-terminal region of S1 (8). Based on structural biology studies, the RBD can be oriented either in the up/standing or down/lying state with the up/standing state associated with higher pathogenicity (9). Polyclonal antibodies to the RBD of the SARS-CoV-2 protein have been shown to inhibit interaction with the ACE2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy (10). It has been demonstrated that the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (11, 12). While the SARS-CoV-2 D614G variant is currently the most prevalent form of the virus, the mechanism of action has not been identified (13).
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