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Z-Phe-Arg-pNA . hydrochloride

Cathepsin substrate
ALX-260-130-M005 5 mg 51.00 USD
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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
Sequence:Z-Phe-Arg-pNA (pNA=p-Nitroanilide)
Formula:C29H33N7O6 . HCl
MW:575.6 . 36.5
Purity:≥99% (TLC)
Appearance:White to off-white powder.
Solubility:Soluble in methanol (50mg/ml) and DMSO.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only

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;

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