A cathepsin substrate
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Suc-AAPF-pNA

Item No. 14993

Technical Information
Formal Name
N-(3-carboxy-1-oxopropyl)-L-alanyl-L-alanyl-L-prolyl-N-(4-nitrophenyl)-L-phenylalaninamide
CAS Number
70967-97-4
Synonyms
  • Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
Molecular Formula
C30H36N6O9
Formula Weight
Purity
≥95%
A crystalline solid
DMF: 5 mg/mlDMSO: 5 mg/mlDMSO:PBS (pH 7.2) (1:1): 0.5 mg/ml
λmax
314 nm
SMILES
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
InChi Code
InChI=1S/C30H36N6O9/c1-18(31-25(37)14-15-26(38)39)27(40)32-19(2)30(43)35-16-6-9-24(35)29(42)34-23(17-20-7-4-3-5-8-20)28(41)33-21-10-12-22(13-11-21)36(44)45/h3-5,7-8,10-13,18-19,23-24H,6,9,14-17H2,1-2H3,(H,31,37)(H,32,40)(H,33,41)(H,34,42)(H,38,39)/t1
InChi Key
LKDMKWNDBAVNQZ-WJNSRDFLSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    Product Description

    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.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    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 alHeparin protects cathepsin G against inhibition by protein proteinase inhibitors. The Journal of Biological Chemisty 269(47), 29502-29508 (1994).

    3. Kofron, J.L., Kuzmic, P., Kishore, V., et alDetermination 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 alSecretory production of recombinant human chymase as an active form in Pichia pastoris. Yeast 16(4), 315-323 (2000).