Skip to main content

Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 10887-CV

Lambda Variant
R&D Systems, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
Loading...
10887-CV-100

Key Product Details

Source

HEK293

Accession #

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived sars-cov-2 Spike protein
SARS-CoV-2 C.37 Spike
(Val16-Lys1211)
(Gly75Val, Thr76Ile, RSYLTPG246-252 del, Asp253Asn, Leu452Gln, Phe490Ser, Asp614Gly, Thr859Asn) (Arg682Ser, Arg685Ser, Lys986Pro, Val987Pro)
Accession # YP_009724390.1
GCN4-IZ 6-His tag
N-terminus C-terminus

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Val16

Predicted Molecular Mass

137 kDa

SDS-PAGE

145-170 kDa, under reducing conditions.

Activity

Measured by its binding ability in a functional ELISA with Recombinant Human ACE-2 His-tag (Catalog # 933-ZN).

Scientific Data Images for Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His Protein, CF

Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His-tag Protein Binding Activity

Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His-tag (Catalog # 10887-CV) binds Recombinant Human ACE-2 His-tag (Catalog # 933-ZN) in a functional ELISA.

Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His-tag Protein SDS-PAGE

2 μg/lane of Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His-tag (Catalog # 10887-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 145-170 kDa.

Formulation, Preparation and Storage

10887-CV
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 500 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: Spike

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% aa 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 with mutations compared to the Wuhan-Hu-1 SARS-CoV-2 reference sequence. First identified in South America in late 2020, the C.37, or Lamda, variant is considered a Variant of Interest (VOI) as it contains several mutations in the RBD domain that potentially affect viral fitness and transmissibility: L452Q and F490S (11). The F490S mutation, along with several mutations at position L452, has been associated with resistance to neutralization by multiple monoclonal antibodies (12).

References

  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. Romero, P.E. et al. (2021) medRxiv https://doi.org/10.1101/2021.06.26.21259487 .
  12. Liu, Z. et al. (2021) Cell Host Microbe. 29:477.

Long Name

Spike Protein

Alternate Names

S Protein

Entrez Gene IDs

918758 (HCoV-229E); 2943499 (HCoV-NL63); 39105218 (HCoV-OC43); 37616432 (MERS-CoV); 1489668 (SARS-CoV); 43740568 (SARS-CoV-2)

Gene Symbol

S

UniProt

Additional Spike Products

Product Documents for Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant SARS-CoV-2 C.37 Spike (GCN4-IZ) His Protein, CF

For research use only

Loading...
Loading...
Loading...