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Recombinant SARS-CoV-2 B.1.1.7 Spike GCN4-IZ His Protein, CF

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Recombinant SARS-CoV-2 B.1.1.7 Spike (GCN4-IZ) His-tag (Catalog # 10796-CV) binds Recombinant Human ACE-2 His-tag (933-ZN) in a functional ELISA.
2 μg/lane of Recombinant SARS-CoV-2 B.1.1.7 Spike GCN4-IZ His-tag (Catalog # 10796-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more
Recombinant SARS-CoV-2 B.1.1.7 (UK Variant) Spike protein (GCN4-IZ) 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 ...read more

Product Details

Summary
Reactivity VSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant SARS-CoV-2 B.1.1.7 Spike GCN4-IZ His Protein, CF Summary

Additional Information
Alpha Variant (UK)
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
SARS-CoV-2 B.1.1.7 Spike
(Val16-Lys1211)(His69del, Val70del, Tyr145del, Asn501Tyr, Ala570Asp, Asp614Gly, Pro681His, Thr716Iso, Ser982Ala, Asp1118His)(Arg682Ser, Arg685Ser, Lys986Pro, Val987Pro)
Accession # YP_009724390.1
GCN4-IZ6-His tag
N-terminusC-terminus
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.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
138 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.
SDS-PAGE
140-170 kDa, under reducing conditions.
Publications
Read Publications using
10796-CV in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant SARS-CoV-2 B.1.1.7 Spike GCN4-IZ His Protein, CF

  • 2019-nCoV S Protein
  • 2019-nCoV Spike
  • COVID-19 Spike
  • E2
  • Human coronavirus spike glycoprotein
  • Peplomer protein
  • S glycoprotein
  • S Protein
  • SARS-COV-2 S protein
  • SARS-COV-2 Spike glycoprotein
  • SARSCOV2 Spike protein
  • SARS-CoV-2
  • Severe Acute Respiratory Syndrome Coronavirus 2 Spike Protein
  • Spike glycoprotein
  • Spike
  • surface glycoprotein

Background

SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that also include MERS-CoV and SARS-CoV-1. Coronaviruses are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M) and Nucleocapsid protein (N) (1). The SARS-CoV-2 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 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 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 a metallopeptidase, Angiotensin-Converting Enzyme 2 (ACE-2), but with much higher affinity and faster binding kinetics through the receptor binding domain (RBD) located in the C-terminal region of S1 subunit (6). It has been demonstrated that the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (7, 8). Polyclonal antibodies to the RBD of the SARS-CoV-2 protein have been shown to inhibit interaction with the ACE-2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy (9). There is also promising work showing that the RBD may be used to detect presence of neutralizing antibodies present in a patient's bloodstream, consistent with developed immunity after exposure to the SARS-CoV-2 (10). Several emerging SARS-CoV-2 genomes have been identified including the B 1.1.7 (United Kingdom) variant (11). The B 1.1.7 variant contains 1 significant mutation of interest in the RBD domain, N501Y, which has been shown to result in enhanced binding affinity for hACE-2 (12). Further, the B 1.1.7 variant appears to more easily transmissible, exhibit increased viral loads and, potentially, be associated with higher mortality rates compared to preexisting variants (11, 13).
  1. Wu, F. et al. (2020) Nature 579:265.
  2. Tortorici, M.A. and D. Veesler (2019) Adv. Virus Res. 105:93.
  3. Bosch, B.J. et al. (2003). J. Virol. 77:8801.
  4. Belouzard, S. et al. (2009) Proc. Natl. Acad. Sci. 106:5871.
  5. Millet, J.K. and G.R. Whittaker (2015) Virus Res. 202:120.
  6. Ortega, J.T. et al. (2020) EXCLI J. 19:410.
  7. Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.
  8. Isabel, et al. (2020) Sci Rep 10, 14031. https://doi.org/10.1038/s41598-020-70827-z.
  9. Tai, W. et al. (2020) Cell. Mol. Immunol. https://doi.org/10.1016/j.it.2020.03.007.1.
  10. Okba, N.M.A. et al. (2020) Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.
  11. Kidd, M. et al. (2021) The Journal of Infectious Diseases https://doi.org/10.1093/infdis/jiab082.
  12. Zahradník, J. et al. (2021) bioRxiv https://doi.org/10.1101/2021.01.06.425392.
  13. Davies, N.G. (2020) medRxiv doi:10.1101/2020.12.24.20248822.

Publications for SARS-CoV-2 Spike (10796-CV)(2)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


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