Novus Biologicals products are now on bio-techne.com

Recombinant SARS-CoV-2 Spike RBD His-tag Protein, CF

Images

 
Recombinant SARS-CoV-2 Spike RBD His-tag (Tn5 Expressed) (Catalog # 10523-CV) has a molecular weight (MW) of 33.2 kDa as analyzed by SEC-MALS, suggesting that this protein is a monomer.  MW may differ from predicted MW ...read more
Recombinant SARS-CoV-2 Spike RBD His-tag (Tn5 Expressed) (10523-CV) binds Recombinant Human ACE-2 His-tag (933-ZN) in a functional ELISA.
2 μg/lane of Recombinant SARS-CoV-2 Spike RBD His-tag (Tn5 Expressed) (10523-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing ...read more
Binding of ACE-2 to SARS-CoV-2 Spike RBD by surface plasmon resonance (SPR). Recombinant SARS-CoV-2 Spike RBD His-tag Protein (Catalog # 10523-CV) was immobilized on a Biacore Sensor Chip CM5, and binding to recombinant ...read more

Product Details

Summary
Reactivity VSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

View Available Formulations
Catalog# & Formulation Size Price
Novus Biologicals is part of Bio-Techne

Shop this product on bio-techne.com

Recombinant SARS-CoV-2 Spike RBD His-tag Protein, CF Summary

Additional Information
Tn5 Insect Cell Expressed, High ACE-2 Binding Analyzed by SEC-MALS
Details of Functionality
Measured by its binding ability in a functional ELISA with Recombinant Human ACE-2 His-tag (Catalog # 933-ZN).
Source
Trichoplusia ni, T. ni (baculovirus)-derived sars-cov-2 Spike RBD protein
Arg319-Phe541, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Arg319
Structure / Form
Monomer
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
26-32 kDa, under reducing conditions
Publications
Read Publication using
10523-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 Spike RBD His-tag 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 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 two distinct peptides, 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). Based on structural biology studies, the receptor binding domain (RBD), located in the C-terminal region of S1, can be oriented either in the up/standing or down/lying state (6). The standing state is associated with higher pathogenicity and both SARS-CoV-1 and MERS can access this state due to the flexibility in their respective RBDs. A similar two-state structure and flexibility is found in the SARS-CoV-2 RBD (7). Based on amino acid (aa) sequence homology, the SARS-CoV-2 S1 subunit RBD has 73% identity with the RBD of the SARS-CoV-1 S1 RBD, but only 22% homology with the MERS S1 RBD. The low aa sequence homology is consistent with the finding that SARS and MERS bind different cellular receptors (8). 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 (9). Before binding to the ACE2 receptor, structural analysis of the S1 trimer shows that only one of the three RBD domains in the trimeric structure is in the "up" conformation. This is an unstable and transient state that passes between trimeric subunits but is nevertheless an exposed state to be targeted for neutralizing antibody therapy (10). 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 (11). 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 virus (12). Lastly, it has been demonstrated the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (13, 14).
  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. Yuan, Y. et al. (2017) Nat. Commun. 8:15092.
  7. Walls, A.C. et al. (2010) Cell 180:281.
  8. Jiang, S. et al. (2020) Trends. Immunol. https://doi.org/10.1016/j.it.2020.03.007.
  9. Ortega, J.T. et al. (2020) EXCLI J. 19:410.
  10. Wrapp, D. et al. (2020) Science 367:1260.
  11. Tai, W. et al. (2020) Cell. Mol. Immunol. https://doi.org/10.1016/j.it.2020.03.007.
  12. Okba, N. M. A. et al. (2020). Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.
  13. Wang, X. et al. (2020) https://doi.org/10.1038/s41423-020-0424-9.
  14. Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.

Publications for Spike RBD (10523-CV)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Adhesion.


Filter By Application
Adhesion
(1)
All Applications
Filter By Species
Human
(1)
All Species

Reviews for Spike RBD (10523-CV) (0)

There are no reviews for Spike RBD (10523-CV). By submitting a review you will receive an Amazon e-Gift Card or Novus Product Discount.
  • Review with no image -- $10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen
  • Review with an image -- $25/€18/£15/$25 CAD/¥150 Yuan/¥2500 Yen

FAQs for Spike RBD (10523-CV) (0)

There are no specific FAQs related to this product. Read our general customer & technical service FAQs.

Additional Spike RBD Products

Blogs on Spike RBD.

Post-COVID Conditions or Long COVID and COVID Long-Haulers
By Jamshed Arslan, Pharm D, PhD Post-acute infection syndrome (PAIS) is a phenomenon where ill effects of an infection persist even after the infection itself is over. PAIS in the case of COVID is called t...  Read full blog post.

Read our latest blog and use the new citation tool on bio-techne.com

Contact Information

Product PDFs

Calculators

Concentration Calculator

The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.

=
÷

Review this Product

Be the first to review our Recombinant SARS-CoV-2 Spike RBD His-tag Protein, CF and receive a gift card or discount.

Bioinformatics

Uniprot