| Identification | Back Directory | [Name]
SUC-ALA-ALA-PRO-PHE-PNA | [CAS]
70967-97-4 | [Synonyms]
SAAPNA
SUC-AAPF-PNA
Cathepsin G substrate
SUC-ALA-ALA-PRO-PHE-PNA
Cathepsin G Substrate I
N-SUCCINYL-ALA-ALA-PRO-PHE-PNA
SUC-ALA-ALA-PRO-PHE-PNA USP/EP/BP
SUC-ALA-ALA-PRO-PHE-PARANITROANILIDE
CATHEPSIN G SUBSTRATE I, COLORIMETRIC
SUCCINYL-ALA-ALA-PRO-PHE-P-NITROANILIDE
N-SUCCINYL-ALA-ALA-PRO-PHE P-NITROANILIDE
N-Succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide
N-succinyl-alanyl-alanyl-prolyl-phenylanaline nitroanilide
SUCCINYL-L-ALANYL-L-ALANYL-L-PROLYL-L-PHENYLALANINE-4-NITROANILIDE
N-Succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine p-nitroanilide
N-SUCCINYL-L-ALANYL-L-ALANYL-L-PROLYL-L-PHENYLALANINE 4-NITROANILIDE
Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide - CAS 70967-97-4 - Calbiochem
N-Succinyl-Ala-Ala-Pro-Phe-pNA, N-Succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine 4-nitroanilide | [Molecular Formula]
C30H36N6O9 | [MDL Number]
MFCD00077161 | [MOL File]
70967-97-4.mol | [Molecular Weight]
624.64 |
| Chemical Properties | Back Directory | [storage temp. ]
−20°C
| [solubility ]
DMF: 25 mg/mL, clear, light yellow
| [form ]
White to off-white solid | [color ]
White to off-white | [BRN ]
4289896 | [Sequence]
{Suc}-Ala-Ala-Pro-Phe-{pNA} | [InChIKey]
LKDMKWNDBAVNQZ-UHYNAWRVNA-N | [SMILES]
N1(CCC[C@H]1C(=O)N[C@H](C(=O)NC1=CC=C([N+]([O-])=O)C=C1)CC1=CC=CC=C1)C(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CCC(=O)O |&1:4,8,30,35,r| |
| Hazard Information | Back Directory | [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. | [Uses]
N-Succinyl-Ala-Ala-Pro-Phe p-nitroanilide has been used as a substrate to determine chymotrypsin activity. | [Biochem/physiol Actions]
N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide is a substrate for subtilisin and proteases. | [References]
[1] K. NAKAJIMA. Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.[J]. The Journal of Biological Chemistry, 1979, 107 1: 4027-4032. DOI: 10.1016/s0021-9258(18)50690-6
[2] J ERMOLIEFF. Heparin protects cathepsin G against inhibition by protein proteinase inhibitors.[J]. The Journal of Biological Chemistry, 1994, 269 47: 29502-29508.
[3] JAMES L. KOFRON. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay[J]. Biochemistry Biochemistry, 1991, 30 25: 6127-6134. DOI: 10.1021/bi00239a007
[4] H NAKAKUBO. Secretory production of recombinant human chymase as an active form in Pichia pastoris.[J]. Yeast, 2000, 16 4: 315-323. DOI: 10.1002/1097-0061(20000315)16:4<315::aid-yea527>3.0.co;2-4 |
|
|