2019-nCoV Spike Protein S1 (P681H) Catalog No: c19S1-G232H

A C-terminal His- tag is used to express the recombinant 2019-nCoV spike protein S1 (P681H) (16-685). The purity of this protein was found to be around 90% by densitometry with a molecular weight of about 130 kDa.

The activity is identified by examining the binding ability of the 2019-nCoV spike protein S1 (P681H) to the immobilized human ACE2 (19-740) protein through a functional ELISA.

Scientific background

Throughout the world, the novel coronavirus SARS-CoV-2 has been responsible for causing the pandemic of respiratory diseases (COVID-19) in 2020.1 The spike glycoprotein (S) of coronavirus is a type I transmembrane protein consisting of two subunits, S1 and S2. This glycoprotein attaches to host cells via the interaction with angiotensin-converting enzyme 2 (ACE2).2

After the S1 subunit of Spike protein binds to the host ACE2, TMPRSS2 cleaves within the S2 subunit or at the S1/S2 boundary to ease the penetration of viral genomes into the host cells.

Among the 14 defined mutations in the UK SARS-CoV-2 variant—also called VUI-2020/01 or lineage B.1.1.7—P618H mutation within the spike protein is detected next to the cleavage site of furin, making it more appropriate for hydrolysis by TMPRSS2 and supplementing the viral fusion.3

Specific activity

The binding of ACE2 (19-740) Protein (A51C2-G341F) to immobilized 2019-nCoV spike protein S1 (P681H) (C19S1-G232H) was determined by functional ELISA.

The binding of ACE2 (19-740) Protein (A51C2-G341F) to immobilized 2019-nCoV spike protein S1 (P681H) (C19S1-G232H) was determined by functional ELISA. Image Credit: SignalChem Biotech Inc.

References

  1. Zhou P, et al: A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020, 579:270–89.
  2. Lan J, et al: Crystal structure of the 2019-nCov spike receptor-binding domain bound with the ACE2 receptor. Nature. 2020, 581:215–220.
  3. Erol A: Erol A. Are the emerging SARS-COV-2 mutations friend or foe? Immunol Lett. 2021, 230:63-64. doi: 10.1016/j.imlet.2020.12.014.