CoV 2019 Nucleocapsid-Mosaic Protein ein is >90% pure as determined SDS-PAGE.
The E.Coli derived recombinant protein contains the Coronavirus 2019 full length nuclepocapsid Mosaic immunodominant regions [ full length N-antigen ], fused to 6xHis tag at C-terminal.
The 2019 novel coronavirus (2019-nCoV), a human-infecting coronavirus causing viral pneumonia, emerged in a Wuhan, China seafood market in December 2019.
2019-nCoV shares 87% identity with the bat-derived SARS-CoV-2 found in Zhoushan, eastern China, in 2018. Despite amino acid variations, 2019-nCoV's receptor-binding domain (RBD) structure resembles that of 2018 SARS-CoV, suggesting potential binding to the human ACE2 receptor (angiotensin-converting enzyme 2).
While bats are suspected as the natural reservoir, an intermediate animal host from the seafood market is also suspected. Research suggests 2019-nCoV's spike glycoprotein is a recombinant of a bat coronavirus and an unknown coronavirus.
This E. coli-derived recombinant protein consists of the full-length Coronavirus 2019 nucleocapsid protein with immunodominant regions (full-length N-antigen), fused to a C-terminal 6xHis tag.
The CoV 2019 Nucleocapsid-Mosaic protein solution is provided in 1x PBS (phosphate-buffered saline).
The CoV 2019 Nucleocapsid-Mosaic protein is shipped on ice packs. Upon receipt, store at -20°C.
The purity of the CoV 2019 Nucleocapsid-Mosaic protein is greater than 90% as determined by SDS-PAGE (sodium dodecyl-sulfate polyacrylamide gel electrophoresis).
Reactivity with SARS infected individuals not tested.
The Coronavirus disease 2019 (COVID-19) pandemic, caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), has had a profound impact on global health and economies. The virus’s nucleocapsid (N) protein plays a crucial role in its life cycle and has become a focal point for vaccine and diagnostic development .
The SARS-CoV-2 nucleocapsid (N) protein is a multifunctional phosphoprotein essential for the virus’s replication and packaging of its RNA genome . It consists of two main domains: the N-terminal domain (NTD) and the C-terminal domain (CTD), connected by an intrinsically disordered region . The N protein is highly immunogenic and is the most abundant protein in the virion .
The N protein is involved in several critical activities post-virus invasion, including:
Due to its high immunogenicity and abundance, the N protein has been a target for developing vaccines and diagnostic tests . Recombinant forms of the N protein, such as the “Coronavirus 2019 Nucleocapsid Mosaic Recombinant,” have been engineered to enhance immune responses and improve diagnostic accuracy .
Recent studies using cryo-electron microscopy and molecular modeling have provided new insights into the structural dynamics of the N protein. These studies have shown that the N protein can form higher-order oligomers, both in the presence and absence of RNA . Understanding these structural dynamics is crucial for developing strategies to inhibit virus assembly and improve therapeutic interventions .