Nucleoprotein/NP Protein, DcCoV (sf9, His)

Dc-CoV Nucleoprotein (NP, N) is a homodimer with nonspecific binding activity toward nucleic acids. NP packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly, enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication through its interactions with the viral genome and membrane protein M. Nucleoprotein/NP Protein, DcCoV (sf9, His) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of Nucleoprotein/NP Protein, DcCoV (sf9, His) is 448 a.a., with molecular weight of ~50.8 KDa.

Dc-CoV Nucleoprotein (NP, N) is a homodimer composed of 448 amino acids in each chain. NP can be divided into two structural domains interspersed with disordered (unstructured) regions: the N-terminal domain (NTD; also called RBD) serves as a putative RNA-binding domain, while the C-terminal domain (CTD; also called DD) is a dimerization domain, both the NTD and the CTD bind to nucleic acids through electropositive regions on their surfaces.
NP is one of the most abundant coronavirus proteins with nonspecific binding activity toward nucleic acids, including ssRNA, single-stranded DNA, and double-stranded DNA, NP can also act as an RNA chaperone. NP packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. NP plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication^[1].

Virus

Sf9 insect cells

C-His

AHN64796 (M1-I448)

/

Approximately 50.8 kDa.

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.