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

Toxicity: Standard Handling (A)

Ac-Asp-Glu-Val-Asp-pNA

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

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.

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