CoV-2 S2
HEK293
Protein is >85% pure as determined SDS-PAGE.
Description
The HEK293 derived recombinant protein contains the Novel Coronavirus 2019-nCoV Spike Glycoprotein S2, Wuhan-Hu-1 strain, amino acids 685-1211 fused to Fc tag at C-terminal.
Product Specs
In December 2019, a novel coronavirus, designated as 2019-nCoV, emerged in Wuhan, China, causing viral pneumonia in humans. The virus was initially linked to a seafood market in the city.
Genetic analysis revealed that 2019-nCoV shares a high degree of similarity (87%) with a bat-derived SARS-like coronavirus (SARS-CoV-2) discovered in Zhoushan, eastern China, in 2018. Notably, both viruses possess a similar receptor-binding domain (RBD) structure, despite some amino acid variations. This structural similarity suggests that 2019-nCoV might utilize the human angiotensin-converting enzyme 2 (ACE2) receptor for cellular entry, akin to SARS-CoV.
While bats are considered the likely reservoir of 2019-nCoV, the intermediary animal host responsible for transmission to humans remains unclear. Preliminary research indicates that the virus's spike glycoprotein exhibits a recombinant pattern, possibly originating from a recombination event between a bat coronavirus and an unknown coronavirus.
This recombinant protein, produced in HEK293 cells, encompasses the S2 subunit (amino acids 685-1211) of the Spike Glycoprotein from the Wuhan-Hu-1 strain of the 2019 Novel Coronavirus (2019-nCoV). It also incorporates an Fc tag fused to its C-terminal end.
The nCoV-S2 protein solution is provided in Dulbecco's Phosphate Buffered Saline (DPBS).
The protein is shipped with ice packs to maintain its temperature during transit. Upon receipt, it should be stored at -20 degrees Celsius (-4 degrees Fahrenheit).
SDS-PAGE analysis indicates that the protein exhibits a purity greater than 85%.
HEK293
Purified by Protein-G chromatographic technique.
Product Science Overview
The spike glycoprotein is a large type I transmembrane protein that protrudes from the surface of the virus. It is composed of two subunits: S1 and S2 . The S1 subunit contains the receptor-binding domain (RBD), which is responsible for binding to the host cell receptor, angiotensin-converting enzyme 2 (ACE2) . The S2 subunit is involved in the fusion of the viral and host cell membranes, facilitating viral entry into the host cell .
The S2 subunit of the spike glycoprotein is particularly important because it contains several conserved regions that are crucial for the fusion process. These regions include the fusion peptide, heptad repeat regions, and transmembrane domain . The S2 subunit’s role in membrane fusion makes it a key target for therapeutic interventions and vaccine development .
The recombinant spike glycoprotein-S2 is a laboratory-produced version of the S2 subunit. It is used in various research applications, including the development of vaccines and therapeutic antibodies. By studying the recombinant S2 subunit, scientists can gain insights into the mechanisms of viral entry and identify potential targets for antiviral drugs .
The spike glycoprotein, particularly the S2 subunit, is a major target for vaccine development. Vaccines that elicit an immune response against the spike protein can potentially neutralize the virus and prevent infection. Several COVID-19 vaccines, including mRNA vaccines, use the spike protein as the primary antigen to stimulate an immune response .
