Caspase 9 active

GWB-45FA68

Available on request

This antibody recognizes only the cleaved caspase 9 (37 kDa). It does not recognize full-length caspase 9 or any other caspase.

0. 2 mg/ml Storage

ICC: Use at a concentration of 10 - 20 µ g/ml. WB: Use at a concentration of 0. 5 - 1 µ g/ml. Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user. Caspases are synthesized as inactive pro-enzymes that are processed to active form in cells undergoing apoptosis. Caspase 9 is an important member of the caspase family. Upon induction of apoptosis Cytochrome c released from mitochondria associates with pro-caspase 9 (47 kDa) and Apaf-1. The complex processes pro-caspase 9 into a large subunit (37 kDa/17 kDa) and a small subunit (10 kDa). Cleaved caspase 9 further processes other caspases including caspase 3 and caspase 6 to initiate a caspase cascade leading to apoptosis. This affinity purified antibody recognizing the active forms of caspase 9 provides a new tool for identifying apoptotic cell populations in both tissue sections and cultured cells.

Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.

Heterotetramer that consists of two anti-parallel arranged heterodimers each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts with the inhibitors BIRC2 BIRC4 BIRC5 and BIRC7.

Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events.

Contains 1 CARD domain.