Caspase-9, active, cleaved (CASP-9, Apoptotic Protease Mch-6, Apoptotic Protease-activating Factor 3, APAF-3, ICE-like Apoptotic Protease 6, ICE-LAP6, CASP9, MCH6)

Caspases, a family of cysteinyl aspartate-specific proteases, are integral components of the cell death machinery (reviewed in Siegal, 2006; and Lavrik et al, 2005). They play a central role in the initiation and execution of apoptotic cell death and in inflammation. They are typically divided into 3 major groups, depending on the structure of their prodomain and their function. Group 1: inflammatory caspases (1, 4, 5, 11, 12, 14). Group II: initiator of apoptosis caspases (2, 8, 9). Group II: effector caspases (3, 6, 7). Caspases are synthesized as zymogens (inactive pro enzyme precursors which require a biochemical change to become active enzymes) with an N-terminal prodomain of variable length followed by a large subunit (p20) and a small subunit (p10). They are activated through proteolytic cleavage at specific asparagine residues that are located within the prodomain, the p10, and p20 subunits. Activation results in the generation of mature active caspases that consist of the heterotetramer p202-p102. Active caspases mediate cell death and inflammation through cleavage of particular cellular substrates that are involved in these processes. Applications: Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested. Recommended Dilutions: Western Blot: 1:1000-1:2000 Immunohistochemistry (Paraffin): 1:1000-1:5000. Can also be used with frozen sections. Immunoprecipitation: 1:50-1:200 Optimal dilutions to be determined by the researcher. Positive Control: Cells or tissues undergoing apoptosis, lymphatic tissues, ischemic brain. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.