Cleaved Caspase-3 (Asp175) Recombinant Rabbit mAb (S-1406-409)

Cleaved Caspase-3 (Asp175) is the ~17/19 kDa proteolytically activated form of human caspase-3 that, once cleaved after Asp175-Ser176 during apoptosis, loses its N-terminal pro-domain, assembles into active hetero-tetramers (p17/p12) and relentlessly hydrolyzes Asp-x bonds in >100 cytoplasmic, nuclear and cytoskeletal substrates—such as PARP, ICAD, ROCK1 and gelsolin—thereby dismantling cellular architecture, inactivating DNA repair, triggering chromatin condensation, membrane blebbing and phosphatidyl-serine exposure, and thus serving as the pivotal executioner caspase whose appearance, detected by the widely used “Asp175” neo-epitope antibody, is universally recognized as an irreversible biochemical signature of cells committed to programmed cell death.