Caspases are cysteine proteases that play central role in apoptosis
The caspase family was discovered by searching human cDNA libraries for sequences homologous to ced-3, a C
Each caspase is synthesized as an inactive proenzyme that is processed by cleavage at asparte residues by another protease or by self-proteolysis
Fas and tumor necrosis factor receptor type 1 (TNFR1) One of their substrates is poly (ADP ribose) polymerase (PARP) Cleave PARP from its 116kDa form to 85kDa residual fragment The cleavage site in PARP is C-terminal to Asp-216 Utilized as basis for highly specific caspase-3 substrates such as Ac(N-acetyl)-DEVD-AFC (7-amino-4-trifluoromethylcourmarin) and Ac(N-acetyl)-DEVD-AMC (7-amino-4-methylcoumarin) as well as caspase-3 aldehyde inhibitor Ac-DEVD-CHO Storage Buffer: 50mM Tris (pH 8.0) with 100mM NaCl and 50mM imidazole Format: Purified