Anti-Caspase-9 CASP9 Antibody

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 TNFα , TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.

Anti-Caspase 9 antibody was raised against a peptide corresponding to 20 amino acids near the center of human Caspase 9. The immunogen is located within amino acids 290-340 of Caspase 9.

Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes.

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) .

Caspase-9 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.