118584-90-0 Usage
Uses
Used in Biochemistry Research:
FMOC-L-LYS(DANSYL)-OH is used as a substrate for fluorometric proteolytic enzyme assays, providing a means to study enzyme kinetics, specificity, and activity. The dansyl group's fluorescence allows for the real-time monitoring of enzymatic reactions, offering a sensitive and quantitative approach to enzyme analysis.
Used in Drug Discovery and Development:
In the pharmaceutical industry, FMOC-L-LYS(DANSYL)-OH can be employed as a tool for the identification and optimization of potential drug candidates targeting proteolytic enzymes. By monitoring the fluorescence changes upon enzyme cleavage, researchers can screen for compounds that modulate enzyme activity, leading to the development of novel therapeutic agents.
Used in Diagnostic Applications:
FMOC-L-LYS(DANSYL)-OH can be utilized in the development of diagnostic assays for various diseases, particularly those involving abnormal proteolytic activity. The dansyl group's fluorescence can be harnessed to create sensitive and specific tests for the detection and monitoring of disease biomarkers, aiding in early diagnosis and treatment.
Used in Education and Training:
In academic settings, FMOC-L-LYS(DANSYL)-OH serves as an educational tool for teaching students about enzyme kinetics, mechanisms, and the principles of fluorescence-based assays. It provides a hands-on experience in conducting experiments and understanding the fundamental concepts of biochemistry and molecular biology.
Check Digit Verification of cas no
The CAS Registry Mumber 118584-90-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,8,5,8 and 4 respectively; the second part has 2 digits, 9 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 118584-90:
(8*1)+(7*1)+(6*8)+(5*5)+(4*8)+(3*4)+(2*9)+(1*0)=150
150 % 10 = 0
So 118584-90-0 is a valid CAS Registry Number.
118584-90-0Relevant articles and documents
Efficient N-terminal labeling of proteins by use of sortase
Williamson, Daniel J.,Fascione, Martin A.,Webb, Michael E.,Turnbull, W. Bruce
supporting information, p. 9377 - 9380 (2012/11/06)
"Sorting out" N-terminal labeling: The reversibility of transpeptidase reactions makes protein N-terminal labeling challenging. Depsipeptide substrates for sortase A release alcohol by-products, which are poor nucleophiles for the reverse reaction, during ligation. Proteins with an unhindered N-terminal glycine residue can be labeled efficiently with only a minimal excess of the labeling reagent (see scheme).
Synthesis of the Rheb and K-Ras4B GTPases
Chen, Yong-Xiang,Koch, Sebastian,Uhlenbrock, Katharina,Weise, Katrin,Das, Debapratim,Gremer, Lothar,Brunsveld, Luc,Wittinghofer, Alfred,Winter, Roland,Triola, Gemma,Waldmann, Herbert
supporting information; experimental part, p. 6090 - 6095 (2010/11/18)
Now available! Farnesylated and carboxymethylated Rheb (see picture) and K-Ras4B GTPases were synthesized in useful amounts by a combination of expressed protein ligation and solid-phase lipopeptide synthesis. The functionality of the proteins was proven by biochemical, biophysical, and cell-based investigations.
Synthese Bor-reicher Lysindendrimere zur Proteinmarkierung in der Elektronenmikroskopie
Qualmann, Britta,Kessels, Michael Manfred,Musiol, Hans-Juergen,Sierralta, Walter Daniel,Jungblut, Peter Wilhelm,Moroder, Luis
, p. 970 - 973 (2007/10/03)
Keywords: Borverbindungen; Dendrimere; Elektronenmikroskopie; Festphasensynthese; Peptide