Caspases are members of the
cysteine aspartic acid-specific protease family, which is
activated by a variety of signals, including death receptor
ligation, DNA damages, serum starvation and stress.
Caspases play a role in chromatin fragmentation into
nucleosome units, and caspase activation is associated
with the unique apoptosis cell morphology of chromatin
condensation, nucleus fragmentation and cytoplasmic
integrity. Active caspase recognizes several molecules as
substrates during apoptosis. For example, ICAD (inhibitor
of caspase-activated deoxyribonuclease) is inactivated
while CAD (caspase-activated deoxyribonuclease) is
indirectly activated by caspase-3. Caspases recognize
specific peptide sequences containing an aspartic acid, and
cleave these substrate proteins immediately following this
aspartic residue. The tetra-peptide sequence “DEVD” is
preferentially recognized by caspase-3 and -7.
Z-DEVD-FMK is a powerful, irreversible and cell
permeable inhibitor for caspase-3 and -7. To
differentiate caspase-3 and caspase-7 activity, please
consider our CaspSelect immunoassay kits (Code No.
BV-K163 or BV-K167).