Description
Z-Leu-Arg-AMC (156192-32-4) is a sensitive Cathepsin K fluorogenic substrate (Km=8μM, kcat/Km=4 x 105 M-1s-1)1-3. It is cleaved more slowly by the following cathepsins (kcat/Km: B (105)4, F (106)4, L (106)4,5, L2/V (104)5, S (105)2,4,5. Also cleaved by malaria parasite proteases berghepain6, vivapain-2 and -37, and falcipain-1, -2, and -36,8,9. Excitation: 365nm, Emission: 440nm.
References
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Br?mme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377
Singh et al. (2007), A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2; Protein Eng. Des. Sel. 20 171
Na et al. (2004), Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax; Biochem. J. 378(Pt2) 529
Goh et al. (2005), Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes; Parasitol. Res. 97 295
Pandey et al. (2004), Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2; J. Biol. Chem. 279 3484
