Phospho-Caspase 9 (Thr125) Polyclonal Antibody

Target Information

Caspase 9 (ICE-like apoptotic protease 6, ICE LAP6, apoptotic protease Mch6, apoptotic protease activating factor 3, Apaf3) is a member of the peptidase family C14 that contains a CARD domain. Caspases are cysteine proteases, expressed as inactive precursors, that mediate apoptosis by proteolysis of specific substrates. Caspase 9 is active as a heterotetramer, is present in the cytosol and, upon activation, translocates to the mitochondria. Caspase 9 is involved in the caspase activation cascade responsible for apoptosis execution and cleaves/activates Caspase 3 and Caspase 6. Further, Caspase 9 is 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. Caspase 9 promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner, and proteolytically cleaves poly(ADP- ribose) polymerase (PARP). Caspase 9 is expressed in variety of human tissues. An isoform of rat Caspase-9 has been identified in which the C terminus of full-length Caspase-9 is replaced with an alternative peptide sequence. Mutations in Caspase 9 affect brain development. In mice, insufficient Caspase 9 have resulted in abnormal cerebrum development and neuron development. In humans, dysfunctional Caspase 9 expression vary from tissue to tissue. Low levels of Caspase 9 may play a role in cancer development and neurodegenerative diseases such as Alzheimer's Disease (AD).