Recombinant SARS-CoV-2 Spike (GCN4-IZ) His Protein, CF
Recombinant SARS-CoV-2 Spike (GCN4-IZ) His Protein, CF Summary
Why choose R&D Systems SARS-CoV-2 Spike Protein with GCN4-IZ?
- Val16-Lys1211 with GCN4-IZ trimerization domain and C-term His tag
- Stabilizing mutations K986P and V987P promote the prefusion conformation.
- Two mutations, R682S and R685S, eliminate a Furin protease cleavage site.
- Guaranteed Bioactivity and High Purity: Bioactivity tested by functional ELISA and purity determined by SDS-PAGE to be greater than 95%.
- Lot-to-Lot Consistency: Stringent QC testing performed on each lot to ensure consistent activity and purity.
- Bulk Quantities Available: Bulk up and save with large mass quantities to meet your research needs. Supply agreements available, partner with us. Please contact us.
- Most Respected, Most Cited Brand in Proteins: With over 35 years of providing the best recombinant proteins to the scientific community, R&D Systems continues to lead the industry in quality, activity, and purity.
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Product Specifications
| SARS-CoV-2 Spike (Val16-Lys1211) (R682S)(R685S)(K986P)(V987P) Accession # YP_009724390.1 | GCN4-IZ | HHHHHH |
| N-terminus | C-terminus | |
Includes trimerization domain GCN4-IZ
Analysis
Product Datasheets
10561-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.
10561-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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2 μg/lane of Recombinant SARS-CoV-2 Spike (GCN4-IZ) His Protein (Catalog # 10561-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 144-175 kDa.
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Recombinant SARS-CoV-2 Spike (GCN4-IZ) His-tag Protein (Catalog # 10561-CV) binds Recombinant Human ACE-2 His-tag (933-ZN) in a functional ELISA.
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Recombinant SARS-CoV-2 Spike protein with a GCN4-IZ domain and 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 0.37 nM and 94.3 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=2.580 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). The S protein of SARS-CoV-2 shares 75% and 29% amino acid (aa) sequence identity with the 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 (6). 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 (7). 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 (8). It has been demonstrated that the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (9, 10). A SARS-CoV-2 variant carrying the S protein aa change D614G has become the most prevalent form in the global pandemic and has been associated with greater infectivity and higher viral load (11, 12).
- 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.
- Ortega, J.T. et al. (2020) EXCLI J. 19:410.
- Yuan, Y. et al. (2017) Nat. Commun. 8:15092.
- Tai, W. et al. (2020) Cell. Mol. Immunol. https://doi.org/10.1016/j.it.2020.03.007.
- 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.
- 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.
Citations for Recombinant SARS-CoV-2 Spike (GCN4-IZ) His Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concern
Authors: Shajahan, A;Pepi, LE;Kumar, B;Murray, NB;Azadi, P;
Scientific reports
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Site Specific N- and O-glycosylation mapping of the Spike Proteins of SARS-CoV-2 Variants of Concern
Authors: A Shajahan, L Pepi, B Kumar, N Murray, P Azadi
Research square, 2022-11-16;0(0):.
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay
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