|Calculated MW||49,37 KDa|
|Other Names||APAF 3;APAF-3;APAF3;Apoptosis related cysteine peptidase;Apoptotic protease activating factor 3;Apoptotic protease Mch 6;Apoptotic protease Mch-6;Apoptotic protease-activating factor 3;CASP 9;CASP-9;CASP9;CASP9_HUMAN;Caspase 9 apoptosis related cysteine peptidase;Caspase 9 Dominant Negative;Caspase 9c;Caspase-9;Caspase-9 subunit p10;Caspase9;ICE LAP6;ICE like apoptotic protease 6;ICE-LAP6;ICE-like apoptotic protease 6;MCH6;PPP1R56;protein phosphatase 1, regulatory subunit 56;RNCASP9|
|Format||Purified mouse monoclonal antibody in PBS(pH 7.4) containing with 0.02% sodium azide,and 50% glycerol.|
|Storage||Store at -20 °C.Stable for 12 months from date of receipt|
|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).|
|Tissue Location||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.|
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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).
Duan H.,et al.J. Biol. Chem. 271:16720-16724(1996).
Srinivasula S.M.,et al.J. Biol. Chem. 271:27099-27106(1996).
Hadano S.,et al.Mamm. Genome 10:757-760(1999).
Srinivasula S.M.,et al.Cancer Res. 59:999-1002(1999).
Izawa M.,et al.Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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