CoV-2 S1 (1-681)
HEK293.
Sterile Filtered clear solution.
Protein is >95% pure as determined SDS-PAGE.
Description
The HEK293 derived recombinant protein contains the Coronavirus 2019-nCoV Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 1-681 fused to Fc tag at C-terminal having a Mw of 76 kDa.
Product Specs
Initially identified in Wuhan, China, in December 2019, the 2019 novel coronavirus (2019-nCoV) is a human coronavirus responsible for causing viral pneumonia. This virus shares significant genetic similarities with the bat-derived SARS-CoV-2, with 87% similarity to a strain discovered in Zhoushan, eastern China. The 2019-nCoV possesses a receptor-binding domain (RBD) structure analogous to that of the 2018 SARS-CoV, suggesting a potential to bind to the human ACE2 receptor (angiotensin-converting enzyme 2). Although bats are considered the likely reservoir of 2019-nCoV, an intermediary animal host, possibly from seafood sold at Wuhan's Huanan Seafood Wholesale Market, is suspected. Research indicates that the 2019-nCoV's spike glycoprotein may be a product of recombination between a bat coronavirus and an unknown coronavirus.
This recombinant protein, derived from HEK293 cells, consists of the S1 subunit of the Coronavirus 2019-nCoV Spike Glycoprotein (Wuhan-Hu-1 strain). It encompasses amino acids 1 to 681 and is fused with an Fc tag at the C-terminus, resulting in a molecular weight of 76 kDa.
The product is a clear solution that has undergone sterile filtration.
The CoV-2 S1 protein solution is provided in phosphate-buffered saline (PBS) with a pH of 7.4.
The protein is shipped using ice packs to maintain a low temperature. Upon receiving the product, it should be stored at -20°C.
SDS-PAGE analysis confirms that the protein purity is greater than 95%.
HEK293.
Purified by Protein-G chromatography technique.
Product Science Overview
The Coronavirus 2019-nCoV, also known as SARS-CoV-2, is the virus responsible for the COVID-19 pandemic. One of the critical components of this virus is the spike (S) glycoprotein, which plays a crucial role in the virus’s ability to infect host cells. The spike glycoprotein is divided into two subunits: S1 and S2. The S1 subunit is particularly important as it contains the receptor-binding domain (RBD) that binds to the host cell receptor, angiotensin-converting enzyme 2 (ACE2).
The spike glycoprotein S1 subunit (1-681) is a recombinant protein that includes the first 681 amino acids of the spike protein. This region is responsible for the initial attachment of the virus to the host cell. The S1 subunit contains the receptor-binding domain (RBD), which directly interacts with the ACE2 receptor on the surface of human cells .
The binding of the S1 subunit to the ACE2 receptor is a critical step in the viral entry process. Once the S1 subunit binds to ACE2, it triggers a series of conformational changes in the spike protein, leading to the fusion of the viral and cellular membranes. This fusion allows the viral RNA to enter the host cell, initiating the infection process .
Recombinant production of the spike glycoprotein S1 subunit involves expressing the protein in a host cell system, such as HEK293 cells. The recombinant protein is typically tagged with a polyhistidine tag at the C-terminus to facilitate purification. The protein is then purified using techniques such as affinity chromatography .
The recombinant spike glycoprotein S1 subunit is used in various research applications, including vaccine development, diagnostic assays, and therapeutic studies. Its ability to bind to the ACE2 receptor makes it a valuable tool for studying the mechanisms of viral entry and for developing interventions to block this process .
The recombinant spike glycoprotein S1 subunit has been extensively used in research to understand the pathogenesis of SARS-CoV-2. Studies have shown that the S1 subunit can activate various cellular pathways, leading to changes in cellular function and survival. For example, the S1 subunit has been found to increase the activity of connexin 43 (Cx43) hemichannels, which can affect intracellular calcium dynamics and ATP release .
Additionally, the S1 subunit has been used in the development of vaccines and therapeutic agents. By targeting the RBD of the S1 subunit, researchers aim to block the interaction between the virus and the ACE2 receptor, thereby preventing viral entry and infection .
