Anti-SARS-CoV-2 Spike RBD (Clone 2196) – HRP

Anti-SARS-CoV-2 Spike RBD (Clone 2196) – HRP

Product No.: LT8010

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Product No.LT8010
Clone
2196
Target
SARS-CoV-2 RBD
Product Type
Recombinant Monoclonal Antibody
Alternate Names
COV2-2196, SARS-CoV-2 Spike RBD Antibody, Receptor Binding Domain Monoclonal Antibody
Isotype
Human IgG1
Applications
ELISA

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Antibody Details

Product Details

Reactive Species
SARS-CoV-2
Virus
Expression Host
HEK-293 Cells
Immunogen
Sequenced from human survivors of COVID-19 (SARS-CoV-2)
Product Concentration
0.5 mg/ml
Formulation
This recombinant HRP-conjugated antibody is formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4, 1% BSA. <b> (Warning: Use of sodium azide as a preservative will inhibit the enzyme activity of horseradish peroxidase)</b>
Storage and Handling
This horseradish peroxidase conjugated monoclonal antibody is stable when stored at 2-8°C. Do not freeze.
Country of Origin
USA
Shipping
Overnight on Blue Ice.
Applications and Recommended Usage?
Quality Tested by Leinco
ELISA
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.

Description

Description

Specificity
Anti-SARS-CoV-2 Spike RBD-HRP, clone 2196, specifically targets an epitope on the SARS-CoV-2 spike protein receptor-binding domain (RBD).
Background
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.

Monoclonal 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.
Antigen Distribution
The spike RBD is expressed on the surface of SARS-CoV-2.
NCBI Gene Bank ID
Research Area
COVID-19
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Infectious Disease
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Seasonal and Respiratory Infections
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Viral
.
IVD Raw Material

References & Citations

1. Zhou, P., Yang, X., Wang, X. et al. Nature 579, 270–273. 2020.
2. Wu, F., Zhao, S., Yu, B. et al. Nature 579, 265–269. 2020.
3. Wrapp D, Wang N, Corbett KS, et al. bioRxiv. 2020.02.11.944462. 2020.
4. Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Cell. 181(2):281-292.e6. 2020.
5. Li W, Zhang C, Sui J, et al. EMBO J. 24(8):1634-1643. 2005.
6. Shang, J., Ye, G., Shi, K. et al. Nature 581, 221–224. 2020.
7. Gui M, Song W, Zhou H, et al. Cell Res. 27(1):119-129. 2017.
8. Walls AC, Tortorici MA, Snijder J, et al. Proc Natl Acad Sci U S A. 114(42):11157-11162. 2017.
9. Hoffmann M, Kleine-Weber H, Schroeder S, et al. Cell. 181(2):271-280.e8. 2020.
10. Huo J, Zhao Y, Ren J, et al. Cell Host Microbe. S1931-3128(20)30351-6. 2020.
11. Tai, W., He, L., Zhang, X. et al. Cell Mol Immunol 17, 613–620. 2020.
12. Cao Y, Su B, Guo X, et al. Cell. 182(1):73-84.e16. 2020.
13. Premkumar L, Segovia-Chumbez B, Jadi R, et al. medRxiv; 2020.
14. Quinlan BD, Mou H, Zhang L, et al. bioRxiv; 2020.
15. Olba NM, Muller MA, Li W, et al. medRxiv; 2020.
Indirect Elisa Protocol

Certificate of Analysis

Disclaimer AlertProducts are for research use only. Not for use in diagnostic or therapeutic procedures.