CoV-2 N (329 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 329 a.a. from the Nucleocapsid protein and fused to GST-6xHis tag at N-terminal and having a Mw. of 63.5 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.
Genetic analysis reveals that 2019-nCoV shares 87% of its identity with the bat-derived severe acute respiratory syndrome coronavirus 2018 (SARS-CoV-2), originally found in Zhoushan, eastern China. Although structurally similar to the 2018 SARS-CoV receptor-binding domain (RBD), slight variations suggest that 2019-nCoV might bind to the human angiotensin-converting enzyme 2 (ACE2) receptor protein.
Bats are considered the likely natural reservoir of 2019-nCoV; however, researchers hypothesize that an intermediary animal host, potentially from the seafood market, played a role in transmission to humans. Genomic analysis indicates that 2019-nCoV might be a recombinant virus, with its spike glycoprotein originating from a combination of bat coronavirus and another unidentified coronavirus.
This recombinant protein is derived from E. coli and encompasses the C-terminal region (329 amino acids) of the Coronavirus 2019 Nucleocapsid protein. It is fused with a GST-6xHis tag at the N-terminal and exhibits a molecular weight of 63.5 kDa.
The product appears as a clear solution that has undergone sterile filtration.
The CoV-2 Nucleocapsid protein solution is provided in a buffer containing 50mM Tris-HCl at pH 8, 1M Urea, and 50% Glycerol.
The CoV-2 Spike Protein is shipped in a cold chain using ice packs. Upon receipt, it should be stored at -20 degrees Celsius.
The purity of the CoV-2 Nucleocapsid protein exceeds 95%, as determined by SDS-PAGE analysis.
E.Coli.
NTA Sepharose-Affinity Purification.
Product Science Overview
The N protein is composed of 329 amino acids and is highly conserved among coronaviruses. It is divided into two main domains:
- N-terminal domain (NTD): Involved in RNA binding.
- C-terminal domain (CTD): Facilitates protein-protein interactions.
These domains are connected by a linker region rich in serine and arginine residues, which is crucial for the protein’s function .
The N protein is essential for several stages of the SARS-CoV-2 life cycle:
- RNA Packaging: It binds to the viral RNA genome, forming a ribonucleoprotein complex that is essential for the packaging of the viral genome into new virions .
- Viral Assembly: It interacts with other viral structural proteins, such as the membrane (M) and envelope (E) proteins, to facilitate the assembly of new virus particles .
- Immune Response: The N protein is highly immunogenic and elicits a strong immune response, making it a potential target for vaccine and diagnostic development .
Recombinant N proteins are produced using various expression systems, such as bacteria, yeast, or mammalian cells. These recombinant proteins are used in research and diagnostic applications, including:
Recent studies have highlighted the importance of the N protein in understanding the pathogenesis of SARS-CoV-2 and developing therapeutic strategies . For instance, mutations in the N protein have been linked to changes in viral replication and pathogenicity . Additionally, structural insights obtained through techniques like cryo-electron microscopy have provided valuable information for drug design .
In conclusion, the Coronavirus 2019 Nucleocapsid (329 a.a.), Recombinant, is a vital component in the study of SARS-CoV-2, offering significant potential for vaccine and diagnostic development, as well as enhancing our understanding of the virus’s life cycle and pathogenicity.
