Recombinant SARS-CoV-2 C.37 Spike RBD His-tag Protein, CF Summary
| Additional Information |
Lambda Variant L452Q, F490S |
| Details of Functionality |
Measured by its binding ability in a functional ELISA. 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 (Leu452Gln, Phe490Ser), 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 |
|
| 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 |
32-38 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 C.37 Spike RBD His-tag Protein, CF
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. 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 receptor binding domain (RBD) in the C-terminus of the S1
subunit has been identified and 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‑CoV (6,7). The low aa sequence homology is consistent with the
finding that SARS and MERS‑CoV bind different cellular receptors (8). The RBD
of SARS-CoV-2 binds a metallopeptidase,
angiotensin-converting enzyme 2 (ACE-2), similar to SARS-CoV-1, but with much higher affinity and faster binding
kinetics (9). Before binding to the ACE-2 receptor, structural analysis of the
S1 trimer shows that only one of the three RBD domains 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 ACE-2
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 (12). Several
emerging SARS-CoV-2 genomes have been identified with mutations in the RBD compared
to the Wuhan-Hu-1 SARS-CoV-2 reference sequence. First identified in South
America in late 2020, the C.37 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 (13). The F490S mutation, along
with several mutations at position L452, has been associated with resistance to
neutralization by multiple monoclonal antibodies (14).
- Wu, F. et al. (2020) Nature 579:265.
- Tortorici, M.A. and D. Veesler (2019) Adv. Virus Res. 105:93.
- Bosch, B.J. et al. (2003) J. Virol. 77:8801.
- Belouzard, S. et al. (2009) Proc. Natl. Acad. Sci. 106:5871.
- Millet, J.K. and G.R. Whittaker (2015) Virus Res. 202:120.
- Li, W. et al. (2003) Nature 426:450.
- Wong, S.K. et al. (2004) J. Biol. Chem. 279:3197.
- Jiang, S. et al. (2020) Trends. Immunol. https://doi.org/10.1016/j.it.2020.03.007.
- Ortega, J.T. et al. (2020) EXCLI J. 19:410.
- Wrapp, D. et al. (2020) Science 367:1260.
- Tai, W. et al. (2020) Cell. Mol. Immunol. https://doi.org/10.1016/j.it.2020.03.007.1.
- Okba, N.M.A. et al. (2020). Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.
- Romero, P.E. et al. (2021) medRxiv https://doi.org/10.1101/2021.06.26.21259487.
- Liu, Z. et al. (2021) Cell Host Microbe. 29:477.
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