201928-42-9
Chemical Structure
Z-Gly-Pro-Arg-AMC hydrochloride
- CAS No.: 201928-42-9
- Formula:C31H38ClN7O7
- Molecular Weight:656.13
InChIKey: WIIZWHSOXXZHRC-UKOKCHKQSA-N
SMILES: CC(C1=CC=C(NC([C@H](CCCNC(N)=N)NC([C@H]2N(CCC2)C(CNC(OCC3=CC=CC=C3)=O)=O)=O)=O)C=C1O4)=CC4=O.Cl
Biological Activity: Z-Gly-Pro-Arg-AMC hydrochloride is an AMC-labeled fluorescent peptide substrate used in various in vitro biochemical assays for proteases. Z-Gly-Pro-Arg-AMC hydrochloride releases free AMC upon cleavage of the Arg-AMC peptide bond by proteases, generating a fluorescent signal. Z-Gly-Pro-Arg-AMC hydrochloride is efficiently hydrolyzed by CatCΔEx and recombinant proMlCtL, and can also serve as a detection substrate for KLK family proteases[1][2][3][4].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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Z-Gly-Pro-Arg-AMC hydrochloride | 99.15% | Z-Gly-Pro-Arg-AMC hydrochloride is an AMC-labeled fluorescent peptide substrate used in various in vitro biochemical assays for proteases. Z-Gly-Pro-Arg-AMC hydrochloride releases free AMC upon cleavage of the Arg-AMC peptide bond by proteases, generating a fluorescent signal. Z-Gly-Pro-Arg-AMC hydrochloride is efficiently hydrolyzed by CatCΔEx and recombinant proMlCtL, and can also serve as a detection substrate for KLK family proteases. | ||||||||||||||||||||
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References
- [1]. Rebernik M, et al. The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease. Protein expression and purification. 2019 May;157:21-27.
- [2]. Ontoria JM, et al. An allosteric inhibitor of the Zika virus NS2B-NS3 protease with oral efficacy in mouse models. Nature communications. 2026 Feb 10;17(1):1439. [Content Brief]
- [3]. Debela M, et al. Structural basis for the Zn2+ inhibition of the zymogen-like kallikrein-related peptidase 10. Biological chemistry. 2016 Dec 01;397(12):1251-1264.
- [4]. Ahn SJ, et al. Molecular cloning, expression, and characterization of cathepsin L from mud loach (Misgurnus mizolepis). Appl Biochem Biotechnol. 2010 Nov;162(7):1858-71.
