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Recombinant SARS-CoV-2 B.1.617.1 Spike RBD His Protein, CF

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Recombinant SARS-CoV-2 B.1.617 Spike RBD His-tag (Catalog # 10846-CV) binds Recombinant Human ACE-2 His-tag (933-ZN) in a functional ELISA.
2 μg/lane of Recombinant SARS-CoV-2 B.1.617 Spike RBD His-tag (Catalog # 10846-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing ...read more
Recombinant SARS-CoV-2 B.1.617.1 India variant double mutant L452R E484Q Spike RBD protein was immobilized on a Biacore Sensor Chip CM5, and binding to recombinant human ACE-2 (933-ZN) was measured at a concentration ...read more

Product Details

Summary
Reactivity VSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant SARS-CoV-2 B.1.617.1 Spike RBD His Protein, CF Summary

Additional Information
Kappa Variant L452R E484Q
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 RBD protein
Arg319-Phe541 (Leu452Arg, Glu484Gln), with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Arg319
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
26 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
31-38 kDa, under reducing conditions

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.1.617.1 Spike RBD His Protein, CF

  • Spike RBD

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 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). A metallopeptidase, angiotensin-converting enzyme 2 (ACE-2), has been identified as a functional receptor for SARS-CoV-2 through interaction with a receptor binding domain (RBD) located at the C-terminus of S1 subunit (6, 7). The RBD of SARS-CoV-2 shares 73% amino acid (aa) identity with the RBD of the SARS-CoV-1, but only 22% aa identity with the RBD of MERS. A SARS-CoV-2 variant (B.1.617.1) carrying the aa substitution L452R and E484Q in the RBD was identified as a prevalent strain in India (8, 9). Whether these mutations in RBD would cause more severe symptom or decrease the efficacy of vaccine-induced immunity is still under investigation.
  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. Li, W. et al. (2003) Nature 426:450.
  7. Wong, S.K. et al. (2004) J. Biol. Chem. 279:3197.
  8. Yadav, P.D. et al. (2021) bioRxiv https://doi.org/10.1101/2021.04.23.441101.
  9. Cherian, S. et al. (2021) bioRxiv https://doi.org/10.1101/2021.04.22.440932.

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