2019nCoV Spike Protein RBD (L452R, T478K) (C19SD-G231FH)

2019nCoV Spike Protein RBD (L452R, T478K) (C19SD-G231FH)

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Description: Recombinant 2019-nCoV Spike protein S1 subunit, RBD (L452R) (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 new SARS-CoV-2 variant identified in California termed as 20C/S:452R or CAL.20C, possesses L452R as one of the three mutations in the spike protein and this mutation could affect the binding of certain therapeutic monoclonal antibodies. 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. Mascola JR, et al: SARS-CoV-2 viral variants - Tackling a moving target. JAMA. Published online February 11, 2021. doi:10.1001/jama.2021.2088.

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.

Product Sheets (By Lot #) :

F3939-4.pdf