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H-LYS(Z)-OBZL HCL is a synthetic chemical compound that serves as a substrate for enzyme activity assays, specifically for the measurement of cathepsin K and L activities. It is designed to be cleaved by these cathepsin enzymes, allowing for the quantification of their activity through fluorescence or absorbance measurements. H-LYS(Z)-OBZL HCL is instrumental in drug discovery and development research, as well as in the study of lysosomal storage diseases and related disorders. As a research tool, H-LYS(Z)-OBZL HCL is valuable for understanding the mechanisms of lysosomal protease activity and for screening potential therapeutic compounds targeting these enzymes.

114331-06-5

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  • L-Lysine,N2-[(phenylmethoxy)carbonyl]-, phenylmethyl ester, monohydrochloride (9CI)

    Cas No: 114331-06-5

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114331-06-5 Usage

Uses

Used in Enzyme Activity Assays:
H-LYS(Z)-OBZL HCL is used as a substrate in enzyme activity assays for the measurement of cathepsin K and L activities. Its cleavage by these enzymes can be quantified using fluorescence or absorbance measurements, providing a reliable method for assessing enzyme activity levels.
Used in Drug Discovery and Development Research:
In the field of drug discovery and development, H-LYS(Z)-OBZL HCL is used as a research tool to understand the mechanisms of lysosomal protease activity. It aids in the screening of potential therapeutic compounds that target cathepsin K and L enzymes, contributing to the advancement of treatments for various diseases.
Used in the Study of Lysosomal Storage Diseases and Related Disorders:
H-LYS(Z)-OBZL HCL is utilized in the study of lysosomal storage diseases and related disorders to investigate the role of cathepsin K and L enzymes in these conditions. By monitoring the activity of these enzymes, researchers can gain insights into the pathophysiology of these diseases and identify potential therapeutic targets.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, H-LYS(Z)-OBZL HCL is used as a research tool for the development of drugs targeting cathepsin K and L enzymes. Its ability to be cleaved by these enzymes and the quantification of this cleavage allows for the assessment of drug efficacy and the optimization of drug candidates.
Used in Biomedical Research:
H-LYS(Z)-OBZL HCL is used in biomedical research as a substrate to study the function and regulation of cathepsin K and L enzymes. This knowledge can contribute to a better understanding of various biological processes and the development of targeted therapies for diseases associated with these enzymes.

Check Digit Verification of cas no

The CAS Registry Mumber 114331-06-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,4,3,3 and 1 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 114331-06:
(8*1)+(7*1)+(6*4)+(5*3)+(4*3)+(3*1)+(2*0)+(1*6)=75
75 % 10 = 5
So 114331-06-5 is a valid CAS Registry Number.
InChI:InChI=1/C21H26N2O4.ClH/c22-18(20(24)26-14-16-8-3-1-4-9-16)12-7-13-19(23)21(25)27-15-17-10-5-2-6-11-17;/h1-6,8-11,18-19H,7,12-15,22-23H2;1H/t18-,19+;

114331-06-5SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name H-LYS(Z)-OBZL HCL

1.2 Other means of identification

Product number -
Other names H-LYS(CBZ)-OBZL HCL

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:114331-06-5 SDS

114331-06-5Relevant articles and documents

Synthesis and Spectroscopic Properties of Fluorinated Coumarin Lysine Derivatives

Shukla, Lakshmi,Moodie, Lindon W. K.,Kindahl, Tomas,Hedberg, Christian

supporting information, p. 4792 - 4799 (2018/04/25)

The site-selective incorporation of fluorescent amino acids into proteins has emerged as a valuable alternative to expressible protein reporters. For successful application, a robust and scalable, yet flexible, route to non-natural amino acids is required. This work describes an improved synthesis of coumarin-conjugated lysine derivatives where fluorinated variants are accessed. These analogues can be utilized at low pH and should find application probing biological processes that operate under acidic conditions.

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