Cathepsin D Substrate

Cell permeable: no

Primary Target
Substrate for cathepsins D and E

Product does not compete with ATP.

Reversible: no

kcat/Km = 15.6 µM⁻¹ sec⁻¹ and 10.9 µM⁻¹ sec⁻¹ for rat gastric cathepsin D and human erythrocyte cathepsin E, respectively

Toxicity: Standard Handling (A)

An internally quenched fluorogenic 11 amino acid peptide that acts as a sensitive and selective substrate for cathepsins D and E (k_cat/K_m = 15.6 µM^-1s^-1 and 10.9 µM^-1s^-1 for rat gastric cathepsin D and human erythrocyte cathepsin E, respectively). Does not act as a substrate for cathepsins B, H, or L. Cleavage occurs at the Phe-Phe amide bond resulting in enhanced fluorescence. Useful for screening cathepsin D and E inhibitors and for determining cathepsin D and E activity in tissue and cell extracts. Excitation max: ~328 nm; emission max: ~393 nm.

An internally quenched fluorogenic 11-mer peptide that acts as a sensitive and selective substrate for cathepsins D and E (k_cat/K_m = 15.6 µM^-1s^-1 and 10.9 µM^-1s^-1 for rat gastric cathepsin D and human erythrocyte cathepsin E, respectively), but not cathepsins B, H, or L . Cleavage occurs between Phe-Phe residues and results in enhanced fluorescence. A useful tool for inhibitors screening or for the determination of cathepsins D and E activities in crude extracts of various tissues and cell lysates.

MOCAc-Gly-Lys-Pro-Ile-Leu-Phe~Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH₂

MOCAc = (7-Methoxycoumarin-4-yl)acetyl

Yasuda, Y., et al. 1999. J. Biochem.126, 260.
Yasuda, Y., et al. 1999. J. Biochem.125, 1137.

Packaged under inert gas

Supplied as a trifluoroacetate salt.

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

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