Caspase-3 Substrate I, Colorimetric

Colorimetric substrate for CPP32/Apopain/Yama (K_m = 9.7 µM) and related cysteine proteases. Sequence is based on the P1-P4 tetrapeptide cleavage site of poly (ADP-ribose) polymerase (PARP) and includes Asp²¹⁶. CPP32 is the protease responsible for the cleavage of PARP. Can be used with Pro-caspase-3 in in vitro assays to measure caspase-9 activity, since caspase-9 activates pro-caspase-3. Cleavage of the substrate can be monitored at 405 nm (ε = 9160 cm^-1M^-1).

Colorimetric substrate for caspase-3 (K_m = 9.7 µM) and related cysteine proteases. Sequence is based on the P₁-P₄ tetrapeptide cleavage site of poly(ADP-ribose) polymerase (PARP) and includes Asp²¹⁶. Caspase-3 is the protease responsible for the cleavage of PARP. Also a substrate for caspase-6, caspase-7, caspase-8, and caspase-10. Cleavage of pNA is monitored colorimetrically at ~405 nm.

Cell permeable: no

Km = 9.7 µM as colorimetric substrate for caspase-3

Primary Target
Caspas-3

Product does not compete with ATP.

Reversible: no

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Ac-Asp-Glu-Val-Asp-pNA

Cardone, M.H., et al. 1998. Science 282, 1318.
Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
Nicholson, D.W., et al. 1995. Nature376, 37.
Lazebnik, Y.A., et al. 1994. Nature371, 346.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Toxicity: Standard Handling (A)