Recombinant SARS-CoV-2 Spike RBD Fc Chimera Protein, CF Summary
| Additional Information |
HEK293 Expressed, High ACE-2 Binding |
| Details of Functionality |
Measured by its binding ability in a functional ELISA with Recombinant
Human ACE-2 His-tag
(Catalog #
933-ZN). Measured by its binding ability in a functional ELISA with Recombinant
Human EMMPRIN/CD147 Fc Chimera
(Catalog #
972-EMN). |
| Source |
Human embryonic kidney cell, HEK293-derived sars-cov-2 Spike RBD protein SARS-CoV2 Spike RBD
(Arg319-Phe541)
Accession # YP_009724390.1 | IEGRMD | Human IgG1
(Pro100-Lys330) | | N-terminus | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
Arg319 |
| Structure / Form |
Disulfide-linked homodimer |
| 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 |
52 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 |
55-66 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 RBD Fc Chimera 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 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). In SARS-CoV-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). Based on structural biology studies, the receptor binding domain
(RBD), located in the C-terminal region of S1, can be oriented either in the
up/standing or down/lying state (6). The standing state is associated with
higher pathogenicity and both SARS-CoV-1 and MERS can access this state due to
the flexibility in their respective RBDs. A similar two-state structure and
flexibility is found in the SARS-CoV-2 RBD (7). Based on amino acid (aa)
sequence homology, the SARS-CoV-2 S1 subunit RBD has 73% identity with the RBD
of the SARS-CoV-1 S1 RBD, but only 22% homology with the MERS S1 RBD. The low aa sequence homology is consistent
with the finding that SARS and MERS bind different cellular receptors (8). The
S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds
Angiotensin-Converting Enzyme 2 (ACE2), but with much higher affinity and
faster binding kinetics (9). Before binding to the ACE2 receptor, structural
analysis of the S1 trimer shows that only one of the three RBD domains in the
trimeric structure 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 ACE2 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 virus (12). Lastly, it has been demonstrated the S Protein
can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (13, 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.
- Yuan, Y. et al. (2017) Nat. Commun. 8:15092.
- Walls, A.C. et al. (2010) Cell 180:281.
- 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.
- Okba, N. M. A. et al. (2020). Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.
- Wang, X. et al. (2020) https://doi.org/10.1038/s41423-020-0424-9.
- Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.
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