Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
A DNA sequence encoding the SARS-CoV-2 (2019-nCoV) Nucleocapsid Protein (Met1-Ala419) was expressed with a polyhistidine tag at the C-terminus.
E. coli cells
> 90 % as determined by SDS-PAGE.
< 1.0 EU per μg protein as determined by the LAL method.
Predicted N Terminal:
The recombinant SARS-CoV-2 (2019-nCoV) Nucleocapsid Protein (His tag) consists of 430 amino acids and predicts a molecular mass of 47.08 kDa.
Protein Storage Buffer:
PBS, 50% glycerol, pH 7.4.
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