Recombinant SARS-CoV-2 B.1.1.318 Spike GCN4-IZ Protein, CF Summary
| Details of Functionality |
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 protein SARS-CoV-2 Spike
(Val16 - Lys1211)(Thr95Ile, Tyr144del, Glu484Lys, Asp614Gly, Pro681His, Asp796His)(Arg682Ser, Arg685Ser, Lys986Pro, Val987Pro)
Accession # YP_009724390.1 | GCN4-IZ | 6-His tag | | N-terminus | | C-terminus | |
|
| Accession # |
|
| 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 |
|
| 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 |
145-165 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 B.1.1.318 Spike GCN4-IZ 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). The S protein of SARS-CoV-2 shares 75% and 29% amino acid 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 with mutations
compared to the Wuhan-Hu-1 SARS-CoV-2 reference sequence have been identified, including
the B.1.1.318 variant. The B.1.1.318 variant is linked to travel in West Africa
and contains E484K, D614G and P681H mutations, which are commonly found in
variants of concern (VOC) (11). The E484K is located in the RBD and has been
identified as a potentially crucial mutation as it creates a new site for hACE-2
binding and enhances binding affinity, has been shown to confer resistance to
several monoclonal antibodies and is responsible for the first confirmed SARS-CoV-2
reinfection (12, 13). The D614G mutation is located nearby to the RBD domain
and has been shown to increase viral infectivity (14). The P618H mutation is
found adjacent to the furin cleavage site and is proposed to enhance S protein
cleavage and increase viral infectivity (15).
- 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.
- Ortega, J.T. et al. (2020) EXCLI J. 19:410.
- Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.
- Isabel, et al. (2020) Sci Rep 10, 14031. https://doi.org/10.1038/s41598-020-70827-z.
- 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.
- Peacock, T.P. et al. (2021) J Gen Virol. 2021 Apr:102.
- Wang, W.B. et al. (2021) bioRxiv https://doi.org/10.1101/2021.02.17.431566.
- Vasques Nonaka, C.K. et al. (2021) Emerg Infect Dis. https://doi.org/10.3201/eid2705.210191.
- Zhang, L. et al. (2020) Nat Commun. 11:6013.
- Lasek-Nesselquist, E. et al. (2021) medRxiv https://doi.org/10.1101/2021.03.10.21253285.
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