Recombinant BatCoV RaTG13 Spike (GCN4-IZ) His Protein, CF

Recombinant BatCoV RaTG13 Spike (GCN4-IZ) His-tag (Catalog # 10688-CV) binds Recombinant Human ACE-2 Fc Chimera (10544-ZN) in a functional ELISA.

2 μg/lane of Recombinant BatCoV RaTG13 Spike (GCN4-IZ) His-tag (Catalog # 10688-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 145-165 kDa.

• Reactivity: V
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant BatCoV RaTG13 Spike (GCN4-IZ) His Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA with Recombinant Human ACE-2 Fc Chimera (Catalog # 10544-ZN).
• Source: Human embryonic kidney cell, HEK293-derived batcov ratg13 Spike protein
  

  BatCoV RaTG13 Spike (Val16-Pro1209) Accession # QHR63300.2	GCN4-IZ	HHHHHH
  N-terminus		C-terminus

• Accession #: QHR63300.2
• 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: 140-160 kDa, under reducing condition

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 BatCoV RaTG13 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. The bat coronavirus RaTG13 was identified as the closest known relative and likely origin for SARS-Cov-2, though how SARS-CoV-2 evolved to infect humans remains unclear. Coronaviruses are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M) and Nucleocapsid protein (N) (1). The S protein is a homotrimeric glycoprotein, with each ~180-kDa monomer consisting of two subunits, S1 and S2, and it mediates membrane fusion and viral entry (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). A metallopeptidase, angiotensin-converting enzyme 2 (ACE2), 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 S protein of RaTG13 shares 76% and 97% amino acid (aa) sequence identity with the S protein of SARS-CoV-1 and SARS-CoV-2, respectively. Despite high aa identity to SARS-CoV-2, five of the six key amino acids involved in ACE2 binding are different in bat RaTG13, leading to >1000 fold weaker binding to human ACE2 (8, 9). Polyclonal antibodies to the RBD of the SARS-CoV-2 S1 subunit have been shown to inhibit interaction with the ACE2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy (10). 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 (11).

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. Malayia, J. et al. (2020) J Med. Virol. https://doi.org/10.1002/jmv.26261.
9. Wrobel, A.G. et al. (2020) Nat. struct. Mol. Biol. https://doi.org/10.1038/s41594-020-0468-7.
10. Tai, W. et al. (2020) Cell. Mol. Immunol. https://doi.org/10.1016/j.it.2020.03.007.
11. Okba, N. M. A. et al. (2020) Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.

Bioinformatics

• Uniprot:
  • QHR63300.2()