Description: 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. N protein 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. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Description: 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. N protein 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. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Description: The SARS Nucleocaspid is a protein that has a crucial structural importance, by making the virions associates with the RNA genome and therefore create a nucleocapsid that has the specific helical form. There has been found 3 different domain structures to the nucleocapsid antigen. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins. 

Description: SARS-Associated Coronavirus Nuclecapsid is an enveloped viral componentthat contains three external structural antigens, the mains are membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a membrenal receptor and mediates membrane fusion to grant viral entry into the target cells. therefore, S-protein has a crucial part in virus infection cycle and is the main target of neutralizing antibodies.

Description: A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019. The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2)  in humans. While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

Description: SARS-CoV-2 (COVID-19) Nucleocapsid Recombinant Protein

Description: SARS-CoV-2 (COVID-19) Nucleocapsid Recombinant Protein

Description: Nucleocapsid (N) protein is the most abundant protein found in coronavirus. CoV N protein is a highly immunogenic phosphoprotein important for viral genome replication and modulation of cell signaling pathways. It was first identified by a research team while they were screening for ADP-ribosylated proteins during coronavirus (CoV) infection (Grunewald M. E., et al. 2017, Virology; 517: 62-68). The array of diverse functional activities accommodated in N protein makes it more than a structural protein but also an interesting target in the development of antiviral therapeutics. Because of the conservation of N protein sequence and its strong immunogenicity, N protein of coronavirus is chosen as a diagnostic tool.

Description: Nucleocapsid (N) protein is the most abundant protein found in coronavirus. CoV N protein is a highly immunogenic phosphoprotein important for viral genome replication and modulation of cell signaling pathways. It was first identified by a research team while they were screening for ADP-ribosylated proteins during coronavirus (CoV) infection (Grunewald M. E., et al. 2017, Virology; 517: 62-68). The array of diverse functional activities accommodated in N protein makes it more than a structural protein but also an interesting target in the development of antiviral therapeutics. Because of the conservation of N protein sequence and its strong immunogenicity, N protein of coronavirus is chosen as a diagnostic tool.

Description: 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. N protein 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. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Description: Nucleocapsid protein is a most abundant protein of coronavirus. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. While screening for ADP-ribosylated proteins during coronavirus (CoV) infection, we identified as the viral nucleocapsid (N) protein. Novel post-translation modification of the CoV N protein that may play a regulatory role for this important structural protein. The array of diverse functional activities accommodated in the hantaviral N protein goes far beyond to be a static structural protein and makes it an interesting target in the development of antiviral therapeutics. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Description: Nucleocapsid protein is a most abundant protein of coronavirus. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. While screening for ADP-ribosylated proteins during coronavirus (CoV) infection, we identified as the viral nucleocapsid (N) protein. Novel post-translation modification of the CoV N protein that may play a regulatory role for this important structural protein. The array of diverse functional activities accommodated in the hantaviral N protein goes far beyond to be a static structural protein and makes it an interesting target in the development of antiviral therapeutics. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Description: SARS Nucleocapsid (aa 1-422) [His], recombinant protein from E. coli.

Description: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), is an enveloped, single-stranded, positive-sense RNA virus that belongs to the Coronaviridae family 1. The SARS-CoV-2 genome, which shares 79.6% identity with SARS-CoV, encodes four essential structural proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid protein (N) 2. The S protein is a transmembrane, homotrimeric, class I fusion glycoprotein that mediates viral attachment, fusion, and entry into host cells 3. Each ~180 kDa monomer contains two functional subunits, S1 (~700 a.a) and S2 (~600 a.a), that mediate viral attachment and membrane fusion, respectively. S1 contains two major domains, the N-terminal (NTD) and C-terminal domains (CTD). In both SARS-CoV and SARS-CoV-2, the CTD contains the receptor-binding domain (RBD), which binds to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells 3-5. The NTD of SARS-CoV-2 does not bind to ACE2 6, and the function of NTD in SARS-CoV-2 infection is not well understood. In other CoVs, the NTD may promote attachment by binding to sugar moieties 7 and might play a role in the conformational change of S2 required for membrane fusion 8. While most neutralizing antibodies target the RBD domain and block receptor binding, potent neutralizing antibodies targeting NTD were isolated from convalescent COVID19 patients 9, identifying the NTD as an attractive candidate for vaccines and therapeutics. In addition, the NTD is a promising antigen for diagnostic tests, as there is only 53.5% homology between the NTD of SARS-CoV-2 and SARS-CoV 10.