2019-nCoV Spike protein RBD (K417T)(C19SD-G239H)
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Description: Recombinant 2019-nCoV Spike protein S1 subunit, RBD (K417T) (319-541) was expressed in CHO cells using a C-terminal his tag.
Species: SARS-CoV-2 Virus
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 data sheet.
Storage, Stability and Shipping :Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Assay Data :Sample activity Data. For specific information on a given lot, see the related technical datasheet.
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). A variant of SARS-CoV-2 carrying K417T, E484K, and N501Y mutations in the RBD was detected in Manaus, Amazonas state Brazil. This variant belongs to P.1 lineage, which descends from an earlier Brazilian variant (B.1.1.28), and has been potentially associated with an increase in transmissibility or propensity for re-infections. E484K and N501Y mutations are of particular concern since they potentially reduce antibody neutralization and increase affinity for ACE2 receptor (2). As 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. 2. Garcia-Beltran WF, et al: Circulating SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity. Preprint. medRxiv. 2021, doi:10.1101/2021.02.14.21251704.
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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