Abcam's Caspase 9 (active) Red Staining Kit provides a convenient means for detecting activated caspase 9 in living cells. The assay utilizes the caspase 9 inhibitor LEHD-FMK conjugated to sulfo-rhodamine (Red-LEHD-FMK) as the fluorescent in situ marker. Red-LEHD-FMK is cell permeable, nontoxic, and irreversibly binds to activated caspase 9 in apoptotic cells. Visit our FAQs page for tips and troubleshooting.
Activation of caspases plays a central role in apoptosis.
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.
Caspase 9 (also known as ICE like apoptotic protease 6 (ICE LAP6), apoptotic protease Mch6, and apoptotic protease activating factor 3 (Apaf3)) is a member of the peptidase family C14 that contains a CARD domain. It is active as a heterotetramer and has been reported to have two isoforms. ProCaspase 9 is approximately 47 kD. It is present in the cytosol and, upon activation, translocates to the mitochondria. Caspase 9 is involved in the caspase activation cascade responsible for apoptosis execution and cleaves/activates Caspase 3 and Caspase 6. It becomes activated when recruited to the Apaf1/cytochrome c complex.