SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies. It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139 kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.
The antibody was developed by immunizing mice with full-length recombinant SARS nucleocapsid protein.
100 ug in 200 ul PBS containing 0.05% sodium azide.
This monoclonal antibody can be used for detection of SARS Nucleocapsid protein in western blot analysis at 0.5-2 ug/ml. The antibody was tested on a cell line transfected with full-length SARS Nucleocapsid cDNA with a predicted Mw 46 kDa.
Store at 4℃, stable for 6 months. For long-term storage, store at -20℃. Western blot analysis of SARS Nucleocapsid in (A) transfected and (B) untransfected mouse melanoma cell lysate using IMG-654 at 0.5 ug/ml.