2019-nCoV Spike protein RBD (L452R, E484Q) (C19SD-G231DH)
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Description: Recombinant 2019-nCoV Spike protein S1 subunit, RBD (L452R, E484Q) (319-541) was expressed in CHO cells using a C-terminal his tag.
Species: SARS-CoV-2
Tag: HIS tag
Expression System: CHO Cells
Sequence: 319-541
Genbank Number: MN908947
Purity: Sample Purity Data. For specific information on a given lot, see the related technical datasheet.
Storage, Stability, and Shipping: Store product at –70oC. For optimal storage, aliquot targets into smaller quantities after centrifugation and store at the recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Molecular Weight: 39 kDa
Gene Aliases : 2019-nCoV RBD, SARS-CoV-2 spike RBD, novel coronavirus spike RBD, nCoV spike RBD.
Scientific Background: The receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein that recognizes the host ACE2 receptor is a major determinant of viral entry and neutralization, and is the most divergent region (1). Lineage B.1.617, also known as the Indian variant carries unique combination of E484Q and L452R mutations in the RBD of the spike protein. L452R mutation has been previously reported in the California variant (B1.429). Mutation at E484 have been detected in the South African (B.1.351), Brazilian (P.1), and NY variants (B.1.526). Viruses harboring these individual mutations have reduced susceptibility to both monoclonal antibodies and convalescent plasma (2). As these new variants displace the first-wave virus, it is pivotal to evaluate their transmissibility, virulence and their possible tendency to escape antibody neutralization (3).
References :
1.Lan J, et al: Crystal structure of the 2019-nCov spike receptor-binding domain bound with the ACE2 receptor. bioRxiv. doi: https://doi.org/10.1101/2020.02.19.956235.
2.Verghese M, et al: Identification of a SARS-CoV-2 variant with L452R and E484Q neutralization resistance mutations. J Clin Microbiol. 2021, JCM.00741-21. doi: 10.1128/JCM.00741-21
3.Starr TN, et al: Molecular dynamic simulation reveals E484K mutation enhances spike RBD-ACE2 affinity and the combination of E484K, K417N and N501Y mutations (501Y.V2 variant) induces conformational change greater than N501Y mutant alone, potentially resulting in an escape mutant. Cell. 2020, 182(5):1295-1310.
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