anti-SARS-CoV-2 Nucleocapsid Rabbit Monoclonal (RM420)

2019-nCoV N Protein

1mg/ml

32160000

liquid

Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide.

Avoid freeze/thaw cycles.

A recombinant 2019-nCov Nucleocapsid protein expressed in E.coli.

Recombinant Antibody. This antibody reacts to 2019-nCov Nucleocapsid protein. Applications: ELISA. Clone: RM420. Isotype: Rabbit IgG. Formulation: Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide. SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. Sequence analysis of the SARS-CoV-2 S protein genome showed that it was only 75% identical with the SARS-CoV S protein. However, analysis of the receptor binding motif (RBM) in the S protein showed that most of the amino acid residues essential for receptor binding were conserved between SARS-CoV and SARS-CoV-2, suggesting that the 2 CoV strains use the same host receptor for cell entry, the receptor angiotensin-converting enzyme 2 (ACE2). The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.

P59595

Vial

SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. Sequence analysis of the SARS-CoV-2 S protein genome showed that it was only 75% identical with the SARS-CoV S protein. However, analysis of the receptor binding motif (RBM) in the S protein showed that most of the amino acid residues essential for receptor binding were conserved between SARS-CoV and SARS-CoV-2, suggesting that the 2 CoV strains use the same host receptor for cell entry, the receptor angiotensin-converting enzyme 2 (ACE2). The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.

Protein A purified.

Rabbit

This antibody reacts to 2019-nCov Nucleocapsid protein.

Non-hazardous

Primary Antibodies

12352203

Stable for at least 1 year after receipt when stored at -20°C.