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 (severe acute respiratory syndrome) is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness, such as the common cold, in humans. 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 glycosilated spike protein (as well as the nucleocapsid protein) can be detected in infected cell culture supernatants with antisera from SARS patients.
100µgs in 200µl PBS containing 0.2% gelatin and 0.05% sodium azide.
Rabbit IgG.
The antibody was developed by immunizing rabbits with synthetic peptides corresponding to amino acids 1124-1140 of the putative SARS Spike glycoprotein (Genbank accession no. NP_828851).
This polyclonal antibody can be used for detection of SARS Spike protein in Western blot. Full-length Spike protein transfected into UM92 cells was used as a positive control and an approximate 139KDa band is detected.
Store at 4°C, stable for 6 months. For long-term storage, store at -20°C.
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