Suc-AAPF-pNA

A cathepsin substrate

Suc-AAPF-pNA is a chromogenic substrate that can be cleaved by cathepsin G (Km = 1.7 mM), subtilisins, chymotrypsin (Km = 60 µM), chymase (Km = 4 mM), and cyclophilin, but not neutrophil elastase.1,2,3,4 Release of p-nitroanilide is monitored at 405-410 nm. This substrate can be used for inhibitor screening and kinetic analysis.

624.7

≥95%

Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide

OC(CCC(N[C@@H](C)C(N[C@@H](C)C(N1CCC[C@H]1C(N[C@@H](CC2=CC=CC=C2)C(NC3=CC=C([N+]([O-])=O)C=C3)=O)=O)=O)=O)=O)=O

C30H36N6O9

70967-97-4

≥ 4 years

DMF: 5 mg/ml DMSO: 5 mg/ml DMSO:PBS (pH 7.2) (1:1): 0.5 mg/ml

1.Nakajima, K. and Powers, J.C. Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. The Journal of Biological Chemisty 254(10), 4027-4032 (1979).
2.Ermolieff, J.,Boudier, C.,Laine, A., et al. Heparin protects cathepsin G against inhibition by protein proteinase inhibitors. J.Biol.Chem 269(47), 29502-29508 (1994).
3.Kofron, J.L.,Kuzmic, P.,Kishore, V., et al. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30(25), 6127-6134 (1991).
4.Nakakubo, H.,Fukuyama, H.,Nakajima, M., et al. Secretory production of recombinant human chymase as an active form in Pichia pastoris. Yeast 16(4), 315-323 (2000).