2019-nCoV Spike protein RBD (Y453F)(C19SD-G234H)
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Description: Recombinant 2019-nCoV Spike protein S1 subunit, RBD (Y453F) (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 also the most divergent region (1). SARS-CoV-2 spike variant with Y453F mutation has been associated with independent outbreaks linked to mink farms in the Netherlands and Denmark. Structure modeling studies have indicated relatively weaker binding of spike glycoprotein Y453F mutant to human ACE2 Spike protein and ability to escape four of the six tested monoclonal antibodies compared to wild type SARS-COV-2 (2). Hence, as the 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. Hayashi T, et al: Effect of RBD mutation (Y453F) in spike glycoprotein of SARS-CoV-2 on neutralizing antibody affinity. bioRxiv 2020; https://doi.org/10.1101/2020.11.27.401893.
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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