Caspase 9 (ready-to-use)

IgG

Human

Caspase 9

PBS pH 7. 4 containing 1%BSA and 0. 1% sodium azide

Ready-to-use for 10 min at RT. Staining of formalin-fixed tissues requires boiling tissue sections in 10mM citrate buffer pH 6. 0 for 10 min followed by cooling at RT for 20 min. Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user. Caspases are cysteine proteases expressed as inactive precursors that mediate apoptosis by proteolysis of specific substrates. Caspases have the ability to cleave after aspartic acid residues. There are two classes of caspases involved in apoptosis; initiators (activation by receptor cluster) and effectors (activation by mitochondrial permeability transition). Proapoptotic signals autocatalytically activate initiator caspases such as Caspase-8 and Caspase-9. Activated initiator caspases then process effector caspases such as Caspase-3 and Caspase-7 which in turn cause cell collapse.

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.