2019-nCoV Spike protein RBD (S477G) (C19SD-G231BH)

2019-nCoV Spike protein RBD (S477G) (C19SD-G231BH)

  • $100.00


Description: Recombinant 2019-nCoV Spike protein S1 subunit, RBD (S477G) (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: The purity of 2019-nCoV Spike protein RBD (S477G) was determined to be >90% by densitometry, approx. MW 39 kDa.

Activity: Binding ability measured in a functional ELISA. 2019-nCoV spike protein RBD (S477G) binds to immobilized human ACE2 (19-740) protein (A51C2-G341F).

Storage and Stability: 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.

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). Mutation at S477 in the RBD region of the spike protein has been found to strengthen the binding of the SARS-CoV-2 spike with the ACE2 receptor (2). 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. Singh A, et al: Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2. Sci Rep. 2021, 11:4320.

3. Starr TN, et al: Molecular dynamic simulation reveals S477G mutation enhances spike RBD-ACE2 affinity and the combination of S477G, 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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