SARS-CoV-2 Spike RBD Antibody [2165] (HRP) Cat. No.: 10-054

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psi-iconSpecifications
SPECIES REACTIVITY: Virus
IMMUNOGEN: Sequenced from human survivors of COVID-19 (SARS-CoV-2). The spike RBD is expressed on the surface of SARS-CoV-2.
TESTED APPLICATIONS: ELISA, IHC
APPLICATIONS: ELISA (Quality Tested by ProSci)
SPECIFICITY: Anti-SARS-CoV-2 Spike RBD-HRP, clone 2165, specifically targets an epitope on the SARS-CoV-2 spike protein receptor-binding domain (RBD). This antibody does not cross-react with the N-terminal domain (NTD) of the spike protein or the RBD of SARS-CoV.

psi-iconProperties
CLONALITY:Monoclonal
ISOTYPE:Human IgG1
CONJUGATE:HRP
PHYSICAL STATE:Liquid
BUFFER:This HRP-conjugated antibody is formulated in 0.01 M phosphate buffered saline (PBS) pH 7.4, 1% BSA. (Warning: Use of sodium azide as a preservative will inhibit the enzyme activity of horseradish peroxidase)
CONCENTRATION:0.5 mg/ml
STORAGE CONDITIONS:This horseradish peroxidase conjugated monoclonal antibody is stable when stored at 2-8˚ C. Do not freeze.

psi-iconAdditional Info
OFFICIAL SYMBOL:S
ALTERNATE NAMES:SARS-CoV-2 Spike RBD Antibody, Receptor Binding Domain Monoclonal Antibody
PROTEIN GI NO.:SARS-CoV-2
USER NOTE:43740568
psi-iconBackground and References
REFERENCES:1) Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), is an enveloped, single-stranded, positive-sense RNA virus that belongs to the Coronaviridae family 1. The SARS-CoV-2 genome, which shares 79.6% identity with SARS-CoV, encodes four essential structural proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid protein (N) 2. The S protein is a transmembrane, homotrimeric, class I fusion glycoprotein that mediates viral attachment, fusion, and entry into host cells 3. Each ~180 kDa monomer contains two functional subunits, S1 (~700 a.a) and S2 (~600 a.a), that mediate viral attachment and membrane fusion, respectively. S1 contains two major domains, the N-terminal (NTD) and C-terminal domains (CTD). The CTD contains the receptor-binding domain (RBD), which binds to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells 3-5. Although both SARS-CoV and SARS-CoV-2 bind the ACE2 receptor, the RBDs only share ~73% amino acid identity, and the SARS-CoV-2 RBD binds with a higher affinity compared to SARS-CoV 3, 6. The RBD is dynamic and undergoes hinge-like conformational changes, referred to as the “down” or “up” conformations, which hide or expose the receptor-binding motifs, respectively 7. Following receptor binding, S1 destabilizes, and TMPRSS2 cleaves S2, which undergoes a pre- to post-fusion conformation transition, allowing for membrane fusion 8, 9. Polyclonal RBD-specific antibodies can block ACE2 binding 10, 11, and anti-RBD neutralizing antibodies are present in the sera of convalescent COVID19 patients 12, identifying the RBD as an attractive candidate for vaccines and therapeutics. In addition, the RBD is poorly conserved, making it a promising antigen for diagnostic tests 13 14. Serologic tests for the RBD are highly sensitive and specific for detecting SARS-CoV-2 antibodies in COVID19 patients 13 15. Furthermore, the levels of anti-RBD antibodies correlated with SARS-CoV-2 neutralizing antibodies, suggesting the RBD could be used to predict an individual's risk of disease 13.
2) Zhou, P., Yang, X., Wang, X. et al. Nature 579, 270–273. 2020.
3) Wu, F., Zhao, S., Yu, B. et al. Nature 579, 265–269. 2020.
4) Wrapp D, Wang N, Corbett KS, et al. bioRxiv. 2020.02.11.944462. 2020.
5) Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Cell. 181(2):281-292.e6. 2020.
6) Li W, Zhang C, Sui J, et al. EMBO J. 24(8):1634-1643. 2005.
7) Shang, J., Ye, G., Shi, K. et al. Nature 581, 221–224. 2020.
8) Gui M, Song W, Zhou H, et al. Cell Res. 27(1):119-129. 2017.
9) Walls AC, Tortorici MA, Snijder J, et al. Proc Natl Acad Sci U S A. 114(42):11157-11162. 2017.
10) Hoffmann M, Kleine-Weber H, Schroeder S, et al. Cell. 181(2):271-280.e8. 2020.
psi-iconCITATIONS
CITATIONS: 1)Huo J, Zhao Y, Ren J, et al. Cell Host Microbe. S1931-3128(20)30351-6. 2020.

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