Anti-Caspase-9

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFalpha, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues. The Cleaved Caspase-9 polyclonal antibody preferntially recognizes (active) cleaved Caspase-9. Whereas the antibody has a strong preference for (active) cleaved Caspase-9, in some cell or tissue systems or techniques the antibody may also recognize the pro form of Caspase-9. Protein function: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf- 1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP- ribose) polymerase (PARP). [The UniProt Consortium]