156192-32-4

Basic information

• Product Name: Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN
• Synonyms: Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN;Z-LEU-ARG-AMC;Z-LEU-ARG-AMC HYDROCHLORIDE
• CAS NO: 156192-32-4
• Molecular Formula: C30H38N6O6
• Molecular Weight: 578.66
• Mol File: 156192-32-4.mol
• Article Data: 0

Chemical Properties

• Appearance: /
• Storage Temp.: Store at 0-5°C
• Solubility: Soluble in DMSO
• Stability: Stable for 2 years from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 3 months. Protect from light!
• CAS DataBase Reference: Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN(CAS DataBase Reference)
• NIST Chemistry Reference: Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN(156192-32-4)
• EPA Substance Registry System: Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN(156192-32-4)

Safety Data

• Hazardous Substances Data: 156192-32-4(Hazardous Substances Data)

Usage

Description

Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN is a sensitive fluorogenic substrate specifically designed for the detection and measurement of cathepsin K activity. It is characterized by its unique structure that allows for efficient and accurate monitoring of the enzyme's function. This substrate exhibits optimal performance with an excitation wavelength of 365nm and an emission wavelength of 440nm, making it a valuable tool in various research and diagnostic applications.

Uses

Used in Research Applications:
Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN is used as a research tool for studying the activity and function of cathepsin K, a lysosomal protease enzyme. Its high sensitivity and specificity make it an ideal candidate for investigating the role of cathepsin K in various biological processes and diseases.
Used in Diagnostic Applications:
In the field of diagnostics, Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN serves as a valuable substrate for the detection and quantification of cathepsin K levels in biological samples. This can be particularly useful in the identification and monitoring of conditions where cathepsin K activity may be altered, such as certain types of cancer or metabolic disorders.
Used in Drug Development:
Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN is used as a screening tool in the development of new drugs targeting cathepsin K. By monitoring the enzyme's activity in the presence of potential drug candidates, researchers can assess the effectiveness of these compounds in inhibiting or modulating cathepsin K function, ultimately leading to the development of novel therapeutics for various diseases.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN is used as a quality control substrate for the assessment of cathepsin K inhibitors. This ensures that the developed drugs have the desired effect on the target enzyme, contributing to the overall safety and efficacy of the therapeutic agents.
Used in Biotechnology Applications:
Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN is also utilized in biotechnology for the optimization of protein expression and purification processes. By monitoring cathepsin K activity during these procedures, researchers can fine-tune the conditions to maximize the yield and quality of the recombinant proteins produced.

References

Bossard et al. (1996), Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification; J. Biol. Chem. 271 12517 Br?mme et al. (1996), Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme; J. Biol. Chem. 271 2126 Linnevers et al. (1997), Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex; Protein Sci. 6 919 Wang et al. (1998), Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization; J. Biol. Chem., 273 32000 Br?mme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377 Singh et al. (2007), A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2; Protein Eng. Des. Sel. 20 171 Na et al. (2004), Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax; Biochem. J. 378(Pt2) 529 Goh et al. (2005), Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes; Parasitol. Res. 97 295 Pandey et al. (2004), Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2; J. Biol. Chem. 279 3484