Human Caspase-9 Antibody Pair
Caspase-9, CASP-9, Apoptotic protease Mch-6, Apoptotic protease-activating factor 3, APAF-3, ICE-like apoptotic protease 6, ICE-LAP6) [Cleaved into: Caspase-9 subunit p35, Caspase-9 subunit p10]
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Caspase 9 (CASP9) is a crucial enzyme in the intrinsic or mitochondrial pathway of apoptosis, playing a pivotal role in programmed cell death. It is activated when cytochrome c is released from the mitochondria in response to various forms of stress or death signals. Structurally, CASP9 consists of an N-terminal caspase recruiting domain (CARD), a large subunit (p35), a linker region containing the caspase cleavage sites, and a small subunit (p10). Upon activation, it forms a heterotetramer composed of two anti-parallel arranged heterodimers, each consisting of a p35 and a p10 subunit. CASP9 is involved in various pathological conditions, including cancer, where it can be activated by chemotherapies, stress agents, and radiation. Capture antibody: 100 µg. Detection antibody: 100 µg