The primary mechanism by which cytotoxic T cells eliminate virally infected cells is by granule exocytosis. The release of cytotoxic granule contents by cytotoxic T lymphocytes (CTL) triggers apoptotic target cell death. CTL granules contain a poreforming protein, perforin, and a group of serine proteases called granzymes. In the classic model, perforins create holes in the target cell membrane, allowing entrance of the granzymes. Granzyme A and B are the predominant granzymes activated after CTL activation, but each act via an independent apoptotic pathway; granzyme B is activated immediately, while granzyme A acts hours later. The physiological substrates for granzyme A in the apoptotic pathwayhave not been identified. Studies involving mice which are deficient in both granzyme A and B suggest a model whereby the granzyme B pathway may have evolved as the major apoptotic pathway with the granzyme A pathway acting as a backup. Granzyme B has been shown to induce apoptosis and to cleave a number of substrates which are similar in specificity to those of the caspase family of proteinases. Granzyme B can cleave substrates, such as DNA-PKcs, and nuclear mitotic apparatus protein (NuMA). Furthermore, Granzyme B can also cleave substrates such as Bid and DFF45 in a caspase-independent fashion. However, further research is needed to delineate the exact role of caspases in cytotoxic T lymphocyte-induced apoptosis involving Granzyme B. Granzyme B migrates at approximately 32 kDa in SDS/PAGE. Clone 2C5/F5 recognizes human and rat granzyme B.
HRP Goat Anti-Mouse Ig RUO 1mLCat No: 554002
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Store undiluted at 4°C.The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Western blot:Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
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