CoV-2-Spike (1-1211)
CHO
Protein is >95% pure as determined SDS-PAGE.
Description
The CHO derived recombinant protein contains the Coronavirus 2019-Spike Full-Length protein, Wuhan-Hu-1 strain, amino acids 1-1211 having a Mw of 134 kDa fused to His tag at C-terminal. The furin cleavage site (682- 685 a.a.) has been mutated from RRAR to SRAS and the transmembrane domain & intravirion part was replaced with a glycine-serine linker + His-tag
Product Specs
The novel coronavirus, responsible for the viral pneumonia outbreak in 2019 (2019-nCoV), was first identified in Wuhan, China, in December 2019. It was linked to a seafood market in the city.
Genetic analysis reveals 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 differences in the receptor-binding domain (RBD), 2019-nCoV appears to utilize the same ACE2 receptor (angiotensin-converting enzyme 2) as the 2018 SARS-CoV to infect human cells.
While bats are considered the likely natural reservoir of 2019-nCoV, intermediate animal hosts, potentially present at the seafood market, are suspected to have played a role in its transmission to humans. Researchers suggest that the virus may have emerged through recombination events between a bat coronavirus and another unknown coronavirus, particularly within the spike glycoprotein region.
This recombinant protein, expressed in CHO cells, encompasses the full-length spike protein of the Wuhan-Hu-1 strain of Coronavirus 2019 (amino acids 1-1211). It has a molecular weight of 134 kDa and includes a C-terminal His tag. Modifications include a mutation of the furin cleavage site from RRAR to SRAS and the replacement of the transmembrane domain and intravirion part with a glycine-serine linker followed by the His-tag.
The CoV-2 spike full-length protein solution is supplied in Dulbecco's Phosphate-Buffered Saline (DPBS).
The CoV-2 Spike Protein is shipped to you frozen on ice packs. When you receive it, it should be stored at -20 degrees Celsius.
The protein has a purity greater than 95% as determined by SDS-PAGE analysis.
CHO
Purified by Metal affinity chromatographic technique.
Product Science Overview
The Coronavirus 2019 Spike (1-1211 a.a.), Recombinant, refers to a specific segment of the spike protein of the SARS-CoV-2 virus, which is responsible for the COVID-19 pandemic. This recombinant protein is a crucial tool in research and vaccine development due to its role in the virus’s ability to infect host cells.
The spike protein of SARS-CoV-2 is a transmembrane protein that plays a key role in the virus’s ability to enter host cells. It is composed of two subunits, S1 and S2:
- S1 Subunit: Contains the receptor-binding domain (RBD) that binds to the host cell receptor, angiotensin-converting enzyme 2 (ACE2).
- S2 Subunit: Facilitates the fusion of the viral and host cell membranes, allowing the viral RNA to enter the host cell .
The recombinant spike protein (1-1211 a.a.) includes both the S1 and S2 subunits, making it a comprehensive representation of the spike protein’s functional regions.
The recombinant spike protein is used extensively in research for several reasons:
- Vaccine Development: It is a key antigen in many COVID-19 vaccines, including mRNA vaccines like Pfizer-BioNTech and Moderna, which use the spike protein to elicit an immune response.
- Diagnostic Tools: It is used in serological assays to detect antibodies against SARS-CoV-2, helping to determine past infection or vaccine-induced immunity.
- Therapeutic Research: It aids in the development of monoclonal antibodies and other therapeutic agents targeting the spike protein .
- ELISA and Lateral Flow Assays: Used as a positive control in these assays to detect antibodies against SARS-CoV-2.
- Neutralization Assays: Helps in evaluating the efficacy of neutralizing antibodies against different variants of SARS-CoV-2.
- Structural Studies: Provides insights into the conformational changes of the spike protein and its interactions with host cell receptors .
