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| | Suc-Ala-Ala-Pro-Phe-PNA Basic information |
| Product Name: | Suc-Ala-Ala-Pro-Phe-PNA | | Synonyms: | N-Succinyl-Ala-Ala-Pro-Phe 4-nitroanilide;succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide;N-succinyl-alanyl-alanyl-prolyl-phenylanaline nitroanilide;N-Succinyl-Ala-Ala-Pro-Phe-pNA, N-Succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine 4-nitroanilide;Cathepsin G Substrate I;N-SUCCINYL-L-ALANYL-L-ALANYL-L-PROLYL-L-PHENYLALANINE 4-NITROANILIDE;N-SUCCINYL-ALA-ALA-PRO-PHE-PNA;N-SUCCINYL-ALA-ALA-PRO-PHE P-NITROANILIDE | | CAS: | 70967-97-4 | | MF: | C30H36N6O9 | | MW: | 624.64 | | EINECS: | | | Product Categories: | amino;ADC Linker | | Mol File: | 70967-97-4.mol |  |
| | Suc-Ala-Ala-Pro-Phe-PNA Chemical Properties |
| Boiling point | 1072.763±65.00 °C(Press: 760.00 Torr)(predicted) | | density | 1.366±0.06 g/cm3(Temp: 25 °C; Press: 760 Torr)(predicted) | | storage temp. | -20°C | | solubility | DMF: 25 mg/mL, clear, light yellow | | pka | 4.691±0.10(predicted) | | 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| |
| Safety Statements | 22-24/25 | | WGK Germany | 3 | | F | 10 | | HS Code | 2933998090 | | Storage Class | 11 - Combustible Solids |
| | Suc-Ala-Ala-Pro-Phe-PNA Usage And Synthesis |
| 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. 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 |
| | Suc-Ala-Ala-Pro-Phe-PNA Preparation Products And Raw materials |
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