CoV-2 N (1-419)
E.Coli
Protein is >95% pure as determined SDS-PAGE.
Description
The E.Colie derived recombinant protein contains the Coronavirus 2019 CoV-2 Nucleocapsid Phosphoprotein, Wuhan-Hu-1 strain, amino acids (1-419) having a Mw of 46.4 kDa and fused to 6xHis tag at C-terminal.
Product Specs
In December 2019, a novel coronavirus, known as 2019-nCoV or COVID-19, emerged in Wuhan, China, causing viral pneumonia. The virus was linked to a seafood market.
Genetic analysis revealed that 2019-nCoV shares a high degree of similarity (87%) with a bat coronavirus, SARS-CoV-2, found in eastern China. Despite some differences, the structure of 2019-nCoV suggests it can bind to the human ACE2 receptor, similar to SARS-CoV.
While bats are considered the likely natural reservoir of 2019-nCoV, an intermediate animal host, potentially from the seafood market, is suspected. Research indicates that 2019-nCoV might be a recombinant virus, with its spike protein originating from a combination of bat and potentially another unknown coronavirus.
This recombinant protein is derived from E. coli and represents the nucleocapsid phosphoprotein of the Wuhan-Hu-1 strain of Coronavirus 2019 (CoV-2). It encompasses amino acids 1-419 and has a molecular weight of 46.4 kDa, including a C-terminal 6xHis tag.
The CoV-2 Nucleocapsid phosphoprotein was lyophilized in a 20mM Na-carbonate buffer with a pH of 9.2.
The lyophilized Cov-2 Nucleocapsid phosphoprotein is shipped at ambient temperature and remains stable for up to two weeks at room temperature. However, for long-term storage, it is recommended to store the desiccated protein below -18°C. After reconstitution, the COV2 protein should be stored at 4°C for up to 7 days. For extended storage, it should be kept below -18°C. Avoid repeated freeze-thaw cycles.
The purity of this protein is greater than 95%, as determined by SDS-PAGE analysis.
To reconstitute the lyophilized CoV-2 protein, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. The reconstituted protein can be further diluted in other aqueous solutions as needed.
E.Coli
Purified by Metal-Afinity chromatographic technique.
MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKED
LKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANK
DGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRN
SSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEAS
KKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSR
IGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQR
QKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQAHHHHHH
Product Science Overview
The N protein of SARS-CoV-2 is composed of 419 amino acids and has a molecular weight of approximately 45.6 kDa . It is a positively charged, unstable, and hydrophobic protein. The protein predominantly exists in a random coil structure (55.13%), with its tertiary structure determined with high reliability (95.76%) .
The N protein is essential for the packaging of the viral RNA genome into ribonucleoprotein (RNP) complexes, which are then assembled into new virus particles . It is the most abundant protein in virions and exhibits high immunogenicity, making it a potential target for vaccine and diagnostic development .
The N protein has been found to have 91% and 49% similarity to the nucleocapsid proteins of SARS-CoV and MERS-CoV, respectively . It is predicted to be predominantly a nuclear protein and contains several phosphorylated sites and potential protein kinase sites, which may significantly affect its function .
Recombinant N proteins are produced using various expression systems to study their structure, function, and potential as diagnostic or therapeutic targets. These recombinant proteins are crucial for understanding the molecular details of viral genome packaging and for developing vaccines and antiviral drugs .
Recent studies have focused on the subcellular localization, physicochemical properties, and biological functions of the N protein. For instance, cells transfected with the SARS-CoV-2 N protein often show a G1/S phase block accompanied by increased expression of certain tubulin proteins . Additionally, the N protein’s involvement in liquid-liquid phase separation (LLPS) has been explored, highlighting its role in the viral life cycle and its potential as an antiviral target .
In conclusion, the SARS-CoV-2 Nucleocapsid protein (1-419 a.a.) is a vital component of the virus, playing a key role in its replication and assembly. Its high immunogenicity and involvement in critical viral processes make it an attractive target for vaccine and diagnostic development.
