anti-Caspase-3 (human), Rabbit Monoclonal (RM250)

Caspase-3 is a member of the interleukin-1 β-converting enzyme family. This cytoplasmic caspase functions as a heterotetramer and has two isoforms (one acts as a dominant negative inhibitor). The proform of this caspase is approximately 32 kD. Activation of caspase-3 requires proteolytic processing of its inactive pro-form into activated p17 and p12 fragments. Caspase-3 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). Caspase-3 is inhibited by c-IAP1, c-IAP2, XIAP, survivin and Livin and activated by Caspase-6, -8 , and -10, granzyme B, Apaf-1 by cleavage into large p17 and small p12 subunits. Caspase-3 has been shown to cleave PARP, huntingtin, androgen receptor, atrophin-1, DNA- PKcs, D4-GDI, hnRNPs C1/C2, U1snRNP, PKC delta, ATM, fodrin, gelsolin, ICAD, RIP, X-IAP, STAT1, topoisomerase I, vimentin, Rb, lamin B, mdm2, and β-catenin. Caspase-3 is important for normal brain development as well as its typical role in apoptosis, where it is responsible for chromatin condensation and DNA fragmentation. Elevated levels of a fragment of Caspase-3, p17, in the bloodstream is a sign of a recent myocardial infarction. Caspase-3 may play a role in embryonic and hematopoietic stem cell differentiation.