Recombinant SARS-CoV Spike RBD Fc Chimera Protein, CF Summary
| Additional Information |
Mammalian CHO Cell Expressed |
| Details of Functionality |
Measured by its binding ability in a functional ELISA with Recombinant
Human ACE-2 His-tag
(Catalog #
933-ZN). |
| Source |
Chinese Hamster Ovary cell line, CHO-derived sars-cov Spike RBD protein SARS-CoV Spike RBD (Arg306-Phe527) Accession # NP_0828851.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | | N-terminus | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
Arg306 |
| 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 |
61-67 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 Spike RBD Fc Chimera Protein, CF
Background
SARS-CoV was discovered in association with cases of
severe acute respiratory syndrome (SARS) that infected more than 8,000 persons
with over 900 fatalities worldwide in 2002-2003 (1). It belongs to a family of
viruses known as coronaviruses that also include MERS and SARS-Cov2 that causes
the global pandemic coronavirus disease 2019 (Covid-19). Coronavirus is commonly comprised of four
structural proteins: Spike protein(S), Envelope protein (E), Membrane protein
(M), and Nucleocapsid protein (N) (1). SARS-CoV S Protein is a type-I trimerized
membrane glycoprotein that mediates membrane fusion and viral entry. 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-CoV
through interaction with a receptor binding domain (RBD) located at the
C-terminus of S1 subunit (5, 6). Based on amino acid (aa) sequence homology,
the RBD domain of SARS-Cov shares 73% and 24% homology with RBD domain of
SARS-CoV2 and MERS, respectively. Before binding to the ACE-2 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
(7). Antibodies to S protein especially the RBD region of SARS-CoV have been
shown to inhibit interaction with the ACE-2 receptor, confirming RBD as an
attractive target for vaccinations or antiviral therapy (8).
- Rota, P.A. et al. (2003) Science 300:1394.
- Bosch, B.J. et al. (2003). J. Virol. 77:8801.
- Belouzard, S. et al. (2009) Proc. Natl. Acad. Sci. USA 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.
- Ortega, J.T. et al. (2020) EXCLI J. 19:410.
- Du, L. el al. (2009) Nat. Rev. Microbiol. 7:226.
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