Recombinant SARS-CoV-2 Spike S2 (GCN4-IZ) His Protein, CF

2 μg/lane of Recombinant SARS-CoV-2 Spike S2 Subunit (GCN4-IZ) His-tag (Catalog # 10590-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 80-100 kDa.

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

Recombinant SARS-CoV-2 Spike S2 (GCN4-IZ) His Protein, CF Summary

• Additional Information: GCN4-IZ trimerization domain,
• Details of Functionality: Bioassay data are not available.
• Source: Human embryonic kidney cell, HEK293-derived sars-cov-2 Spike S2 Subunit protein
  

  SARS-CoV-2 Spike S2 Subunit (Ser686-Lys1211) Accession # YP_009724390.1	GCN4-IZ	HHHHHH
  N-terminus		C-terminus

• Accession #: YP_009724390.1
• N-terminal Sequence: Ser686
• 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: 63 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: 80-100 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 Spike S2 (GCN4-IZ) His Protein, CF

• COVID-19
• S2 protein
• SARS-CoV-2 Spike
• SARS-CoV-2
• Spike glycoprotein Subunit 2
• Spike protein S2
• spike protein
• Spike S2 Subunit
• structural protein
• 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 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). 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). 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 (2-4). A metallopeptidase, angiotensin-converting enzyme 2 (ACE-2), has been identified as a functional receptor for SARS-CoV2, similar to SARS-CoV-1, through interaction with a receptor binding domain (RBD) located at the C-terminus of S1 subunit (5, 6). The S2 subunit of SARS-CoV-2 shares 90% and 41% amino acid sequence identity with the S2 subunit of SARS-CoV-1 and MERS, respectively. It has been demonstrated the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (7, 8).

1. Rota, P.A. et al. (2003) Science 300:1394.
2. Bosch, B.J. et al. (2003). J. Virol. 77:8801.
3. Belouzard, S. et al. (2009) Proc. Natl. Acad. Sci. USA 106:5871.
4. Millet, J.K. and G. R. Whittaker (2015) Virus Res. 202:120.
5. Li, W. et al. (2003) Nature 426:450.
6. Wong, S.K. et al. (2004) J. Biol. Chem. 279:3197.
7. Wang, X. et al. (2020) https://doi.org/10.1038/s41423-020-0424-9.
8. Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v.

Bioinformatics

• Uniprot:
  • YP_009724390.1(Llama)