88899-22-3 Usage
Uses
Used in Research and Pharmaceutical Development:
BZ-PHE-VAL-ARG-AMC is used as a diagnostic tool for measuring the activity of proteolytic enzymes such as trypsin and chymotrypsin. Its application is crucial in understanding the role of these enzymes in various biological processes and their potential as therapeutic targets.
Used in Enzyme Activity Assays:
BZ-PHE-VAL-ARG-AMC is used as a substrate in enzymatic assays to determine the activity levels of proteolytic enzymes. The cleavage of the peptide by the enzyme releases the AMC group, which emits a strong fluorescence signal. This signal can be measured to quantify the enzymatic activity, providing valuable data for research and drug development.
Used in Studying Enzyme Inhibitors:
BZ-PHE-VAL-ARG-AMC is also used in the study of enzyme inhibitors that target proteolytic enzymes. By monitoring the fluorescence signal in the presence of potential inhibitors, researchers can evaluate the effectiveness of these compounds in inhibiting enzymatic activity, which is essential for the development of new therapeutic agents.
Used in Quality Control and Standardization:
In the pharmaceutical industry, BZ-PHE-VAL-ARG-AMC is used for quality control and standardization of proteolytic enzyme preparations. The consistent fluorescence signal produced upon enzymatic cleavage allows for accurate measurement and comparison of enzyme activity across different samples, ensuring the reliability and efficacy of enzyme-based therapeutics.
Check Digit Verification of cas no
The CAS Registry Mumber 88899-22-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,8,8,9 and 9 respectively; the second part has 2 digits, 2 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 88899-22:
(7*8)+(6*8)+(5*8)+(4*9)+(3*9)+(2*2)+(1*2)=213
213 % 10 = 3
So 88899-22-3 is a valid CAS Registry Number.
88899-22-3Relevant academic research and scientific papers
Beythien, Joerg,Barthélémy, Sophie,Schneeberger, Peter,White, Peter D.
, p. 3009 - 3012 (2006)
A novel linker strategy for the efficient side-chain anchoring of arginine is described. The utility of this approach was demonstrated by the facile synthesis of arginine-specific fluorogenic peptide substrates by standard Fmoc solid phase peptide synthesis methods.
