Recombinant SARS-CoV-2 D614G Spike His-tag, Protein CF
Recombinant SARS-CoV-2 D614G Spike His-tag, Protein CF Summary
Product Specifications
Val16-Lys1211 (Asp614Gly, Arg682Ser, Arg685Ser, Lys986Pro, Val987Pro), with a C-terminal 6-His tag
Analysis
Product Datasheets
10620-CV
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
10620-CV
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Recombinant SARS-CoV-2 D614G Spike His-tag (Catalog # 10620-CV) binds Recombinant Human ACE-2 His-tag (933-ZN) in a functional ELISA.
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2 μg/lane of Recombinant SARS-CoV-2 D614G Spike His-tag, Protein (Catalog # 10620-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 150-170 kDa.
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Recombinant SARS-CoV-2 Spike protein D614G His-tag was immobilized on a Biacore Sensor Chip CM5, and binding to recombinant human ACE-2 (933-ZN) was measured at a concentration range between 0.092 nM and 47.2 nM. The double-referenced sensorgram was fit to a 1:1 binding model to determine the binding kinetics and affinity, with an affinity constant of KD=2.099 nM.
Background: Spike
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). It has been demonstrated that the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (9, 10). It is proposed that the D614G mutation introduces an additional elastase cleavage site near the S1-S2 junction and this additional processing helps with viral entry (11).
- Wu, F. et al. (2020) Nature 579:265.
- Tortorici, M.A. and D. Veesler (2019) Adv. Virus Res. 105:93.
- Bosch, B.J. et al. (2003) J. Virol. 77:8801.
- Belouzard, S. et al. (2009) Proc. Natl. Acad. Sci. 106:5871.
- Millet, J.K. and G.R. Whittaker (2015) Virus Res. 202:120.
- Korber, B. et al. (2020) Cell 182:812.
- Zhang, L. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.06.12.148726v1.
- Ortega, J.T. et al. (2020) EXCLI J. 19:410.
- Wang, X. et al. (2020) https://doi.org/10.1038/s41423-020-0424-9.
- Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.
- Bhattacharyya, C. et al. (2020) bioRxiv https://doi.org/10.1101/2020.05.04.075911.
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