Replaces Prod. #: BML-P140
Chromogenic substrate for Cathepsins B, K, L, and S, papain, trypsin, and plasma kallikrein. This substrate is likely to be cleaved by other cathepsins (see Z-Phe-Arg-AMC). Release of pNA is monitored at 405-410 nm (pNA ε410=8800 M-1cm-1). Useful for inhibitor screening and kinetic analysis.
Product Details
| Alternative Name: | Z-FR-pNA . HCl |
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| Sequence: | Z-Phe-Arg-pNA (pNA=p-Nitroanilide) |
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| Formula: | C29H33N7O6 . HCl |
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| MW: | 575.6 . 36.5 |
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| CAS: | 59188-54-4 |
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| Formulation: | Lyophilized |
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| Purity: | ≥99% (TLC) |
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| Appearance: | White to off-white powder. |
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| Solubility: | Soluble in methanol (50mg/ml) and DMSO. |
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| Shipping: | Ambient Temperature |
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| Long Term Storage: | -20°C |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Modulation of Cystatin C in Human Macrophages Improves Anti-Mycobacterial Immune Responses to Mycobacterium tuberculosis Infection and Coinfection With HIV: D. Pires, et al.; Front. Immunol.
18, 742822 (2021),
Abstract;
Protective effects of L-carnitine on behavioral alterations and neuroinflammation in striatum of glutaryl-COA dehydrogenase deficient mice: G. Guerreiro, et al.; Arch. Biochem. Biophys.
709, 108970 (2021),
Abstract;
Cloning and characterization of a basic cysteine-like protease (cathepsin L1) expressed in the gut of larval Diaprepes abbreviatus L.(Coleoptera: Curculionidae): S. Ben-Mahmoud, et al.; J. Insect Physiol.
72, 1 (2015),
Abstract;
Expression of a Codon-Optimized Carica papaya Papain Sequence in the Methylotrophic Yeast Pichia pastoris: N. Werner, et al.; J. Microb. Biochem. Technol.
7, 1948 (2015),
Application(s): In vitro activation and Z-FR-pNa hydrolysis assay,
Full Text
Photometric or fluorometric assay of cathepsin B, L and H and papain using substrates with an aminotrifluoromethylcoumarin leaving group: J.R. Tchoupe, et al.; Biochim. Biophys. Acta
1076, 149 (1991),
Abstract;
General Literature References
Novel, nonpeptidic cyanamides as potent and reversible inhibitors of human cathepsins K and L.: J.P.Falgueyret et al.; J. Med. Chem.
44, 94 (2001),
Abstract;
Acidic pH as a physiological regulator of human cathepsin L activity.: B. Turk et al.; Eur. J. Biochem.
259, 926 (1999),
Abstract;
Subtilisin and alpha-chymotrypsin catalyzed synthesis of peptides containing arginine and lysine p-nitroanilides as C-terminal moieties.: V. Stepanov et al.; Bioorg. Med. Chem.
3, 479 (1995),
Abstract;
Kinetics of the pH-induced inactivation of human cathepsin L.: B. Turk et al.; Biochemistry
32, 375 (1993),
Abstract;
The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B.: D. Bromme et al.; Biochem. J.
264, 475 (1989),
Abstract;
