Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).
Description: Total cell lysates from Rat glioma C6 cells, untreated or treated with 1 mM staurosporine to activate apoptotic cascades and induce proteolytic cleavage of various apoptosis-related proteins including caspases and PARP. This lysate pair is produced as a molecular weight control for western blotting. Boil lysates for 2 minutes in the original tube, then load 10-15 ml per mini-gel lane.
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