Anti-Caspase 9/CASP9 Antibody Picoband® (Biotine Conjugate)

CASP9 (CASPASE9), also called APAF3, is an initiator caspase, encoded by the CASP9 gene. The CASP9 gene is mapped to chromosome 1p36.3-p36.1 by FISH. CASP9 is identified as a member of the caspase family that participates in caspase-3 activation in vitro. And it also regarded as the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP. Its genomic coordinates (GRCh37) is 1:15,818,768-15,851,284. The crystal structure of CASP9 is complex with the BIR3 in an inhibitory domain of XIAP at 2.4-angstrom resolution and the CASP9 gene contains 9 exons and spans approximately 35 kb of genomic DNA. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation. CASP9 activity increases dramatically upon association with the apoptosome complex. And the majority of Casp9 knockout mice died perinatally with a markedly enlarged and malformed cerebrum caused by reduced apoptosis during brain development.

Caspase-9;CASP-9;3.4.22.62;Apoptotic protease Mch-6;Apoptotic protease-activating factor 3;APAF-3;ICE-like apoptotic protease 6;ICE-LAP6;Caspase-9 subunit p35;Caspase-9 subunit p10;CASP9;MCH6;

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).

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.