HEK293
Protein is >95% pure as determined SDS-PAGE.
The HEK293 derived recombinant protein contains the Coronavirus 2019-Spike N-Terminal Domain, Wuhan-Hu-1 strain, amino acids 1-260 fused to Fc tag at C-terminal.
In December 2019, a novel coronavirus, designated as 2019-nCoV, emerged in Wuhan, China, causing viral pneumonia in humans. The virus was 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. Despite some genetic variations, the receptor-binding domain (RBD) of 2019-nCoV closely resembles that of the 2018 SARS-CoV, suggesting its potential to bind to the human ACE2 receptor (angiotensin-converting enzyme 2).
While bats are considered the likely natural reservoir of 2019-nCoV, the presence of other animals at the seafood market raised suspicions of an intermediate host. Research suggests that 2019-nCoV might be a recombinant virus, with its spike glycoprotein originating from a recombination event between a bat coronavirus and an unknown coronavirus.
This recombinant protein is derived from HEK293 cells and encompasses the N-terminal domain (amino acids 1-260) of the Wuhan-Hu-1 strain of the Coronavirus 2019 Spike protein. It is fused with an Fc tag at its C-terminus.
The CoV-2 spike protein solution is provided in Dulbecco's Phosphate-Buffered Saline (DPBS).
The CoV-2 Spike Protein is shipped using ice packs to maintain a low temperature. Upon receiving the protein, it should be stored at -20 degrees Celsius.
The purity of the protein exceeds 95%, as determined by SDS-PAGE analysis.
HEK293
Purified by Protein-G chromatographic technique.
The Coronavirus 2019 Spike (1-260 a.a.), Recombinant, refers to a specific segment of the spike protein of the SARS-CoV-2 virus, which causes COVID-19. This segment includes the first 260 amino acids (a.a.) of the spike protein, which plays a crucial role in the virus’s ability to infect host cells.
The spike protein of SARS-CoV-2 is a transmembrane protein that protrudes from the viral surface, giving the virus its characteristic crown-like appearance. 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 facilitates the fusion of the viral and host cell membranes, allowing the viral RNA to enter the host cell.
The segment comprising the first 260 amino acids is part of the S1 subunit and includes the N-terminal domain (NTD) and part of the RBD. This region is critical for the initial attachment of the virus to the host cell.
Recombinant proteins are produced by inserting the gene encoding the protein of interest into an expression system, such as bacteria, yeast, or mammalian cells. For the Coronavirus 2019 Spike (1-260 a.a.), Recombinant, the gene encoding the first 260 amino acids of the spike protein is cloned into an expression vector, which is then introduced into the host cells. The host cells produce the recombinant protein, which can be purified and used for various applications.