CoV-2 N (127 a.a.)
E.Coli.
Sterile Filtered clear solution.
CoV-2 Nucleocapsid protein is >95% pure as determined SDS-PAGE.
Description
The E.Coli derived recombinant protein contains the Coronavirus 2019 C-terminal region 127 a.a. from the Nucleocapsid protein and fused to GST-6xHis tag at N-terminal and having a Mw. of 39.4 kDa.
Product Specs
In December 2019, a novel coronavirus, 2019-nCoV, responsible for causing viral pneumonia in humans, emerged in Wuhan, China. Its origin was traced back to a seafood market.
Genetic analysis revealed an 87% similarity between 2019-nCoV and the bat-derived SARS-CoV-2 discovered in Zhoushan, eastern China, in 2018. Despite some amino acid variations, the receptor-binding domain (RBD) structure of 2019-nCoV closely resembles that of 2018 SARS-CoV, suggesting a potential interaction with the human ACE2 receptor (angiotensin-converting enzyme 2).
While bats are considered the likely reservoir of 2019-nCoV, researchers hypothesize that an intermediary animal species sold at the market might have played a role in its transmission to humans. Studies indicate that the virus's spike glycoprotein is a product of recombination between a bat coronavirus and an unknown coronavirus.
This recombinant protein, derived from E. coli, encompasses the C-terminal 127 amino acids of the Coronavirus 2019 Nucleocapsid protein. It is fused to a GST-6xHis tag at the N-terminal and has a molecular weight of 39.4 kDa.
The product is a clear solution that has undergone sterile filtration.
The CoV-2 Nucleocapsid protein solution is provided in a buffer consisting of 50mM Tris-HCl at pH 8, 1M Urea, and 50% Glycerol.
The product is shipped with ice packs to maintain its stability. Upon receipt, it should be stored at -20°C.
The purity of the CoV-2 Nucleocapsid protein is greater than 95% as determined by SDS-PAGE analysis.
E.Coli.
NTA Sepharose-Affinity Purification.
Product Science Overview
The Coronavirus 2019 (COVID-19) pandemic has had a profound impact on global health and economies. The causative agent, SARS-CoV-2, has been extensively studied to develop effective diagnostics, treatments, and vaccines. Among the various proteins encoded by the SARS-CoV-2 genome, the nucleocapsid (N) protein plays a crucial role in the viral life cycle and has become a significant target for research and development.
The SARS-CoV-2 nucleocapsid protein is a structural protein that binds to the viral RNA genome, forming a ribonucleoprotein complex. This complex is essential for the packaging of the viral genome into new virions. The N protein is composed of two major domains: the N-terminal domain (NTD) and the C-terminal domain (CTD), which are flanked by intrinsically disordered regions . The N protein is highly conserved among coronaviruses and is known for its high immunogenicity .
The N protein is involved in several critical functions during the SARS-CoV-2 life cycle. It aids in the replication and transcription of the viral RNA, packaging of the RNA into new virions, and modulation of the host cell’s response to infection . The N protein’s ability to bind RNA is crucial for these processes, and it has been shown to preferentially bind single-stranded RNA in a sequence-independent manner .
Recombinant forms of the SARS-CoV-2 N protein have been developed for various research and diagnostic purposes. These recombinant proteins are typically expressed in bacterial systems and purified for use in assays. The recombinant N protein can be used to develop enzyme-linked immunosorbent assays (ELISAs) for detecting antibodies against SARS-CoV-2, which is essential for serological studies and vaccine efficacy assessments .
The high immunogenicity of the N protein makes it an excellent candidate for diagnostic assays. ELISAs using recombinant N protein can detect antibodies in human and animal sera, providing valuable information about immune responses to SARS-CoV-2 infection . Additionally, the N protein’s role in the viral life cycle makes it a potential target for antiviral drug development .
