Calpain-1 Substrate, Fluorogenic

An internally quenched fluorogenic substrate peptide derived from the calpain-1 cleavage site of α-spectrin. It is not recognized by trypsin or α-chymotrypsin and serves as a sensitive and specific substrate for calpain-1 (K_m = 4.6 µM; k_cat = 11 s^-1). Cleavage occurs at the Tyr-Gly bond and results in enhanced fluorescence. Excitation max: ~490 nm; emission max: ~518 nm.

An internally quenched fluorogenic substrate peptide derived from the calpain-1 cleavage site of α-spectrin. It is not recognized by trypsin or α-chymotrypsin and serves as a sensitive and specific substrate for calpain-1 (K_m = 4.6 µM; k_cat = 11 s^-1). Cleavage occurs between Tyr-Gly residues and results in enhanced fluorescence.

Cell permeable: no

Primary Target
A sensitive and specific substrate for calpain-1

Product does not compete with ATP.

Reversible: no

Packaged under inert gas

Toxicity: Standard Handling (A)

H-Lys(FAM)-Glu-Val-Tyr~Gly-Met-Met-Lys(DABCYL)-OH

Supplied as a trifluoroacetate salt.

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Mittoo, S., et al. 2003. Anal. Biochem.319, 234.

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