Caspase-9 inhibitor Z-LEHD-FMK

Caspase is a member of the cysteine aspartic acid-specific protease family, which is activated by a variety of signals of death receptor ligation, DNA damages, serum starvation and stresses etc. Active caspase recognizes a lot of several molecules as substrates to cleave them, occurring to biological events corresponding to the apoptosis. For example, ICAD (inhibitor of caspase-activated deoxyrubonucrease) is inactivated and CAD (caspase-activated deoxyrubonucrease) is indirectly activated by caspase-3, and it is related to chromatin fragmentation for nucleosome units. Caspase recognizes several structural proteins as a substrate to cleave them, and the cleavage is associated with the unique apoptosis cell morphology of chromatin condensation, nucleus fragmentation and cytoplasmic integrity. Tetra peptide sequence ?LEHD? is preferentially recognized by caspase-9. Z-LEHD-FMK is an irreversible and cell permeable powerful inhibitor for caspase-9.

Human: 836 Mouse: 12367

Caspase-9