211990-57-7 Usage
Description
AC-IETD-AFC, also known as N-Acetyl-Ile-Glu-Thr-Asp-7-amino-4-(trifluoromethyl)coumarin, is a fluorogenic substrate specifically designed for the detection and measurement of caspase activity. It is based on the procaspase-3 cleavage site and is utilized in various research applications to study apoptosis and caspase-mediated cell death pathways.
Uses
Used in Research and Development:
AC-IETD-AFC is used as a research tool for the detection and quantification of caspase activity, particularly caspases -6, -8, and -10. It is employed in various experimental setups, including cell-based assays and biochemical analyses, to study the role of caspases in apoptosis and cell death mechanisms.
Used in Drug Discovery and Development:
AC-IETD-AFC serves as a valuable substrate for the identification and evaluation of potential inhibitors or activators of caspases, which can be crucial in the development of therapeutic agents targeting apoptosis-related diseases and conditions.
Used in Diagnostic Applications:
AC-IETD-AFC can be employed in the development of diagnostic tests to assess caspase activity levels in biological samples, which may be indicative of certain diseases or conditions related to apoptosis and cell death.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, AC-IETD-AFC is used as a substrate for the screening and optimization of compounds targeting caspase enzymes. This helps in the development of novel drugs that can modulate caspase activity for therapeutic purposes.
Used in Biotechnology Industry:
AC-IETD-AFC is utilized in the biotechnology industry for the development of biosensors and high-throughput screening platforms to study caspase-mediated cell death pathways and identify potential therapeutic targets.
Used in Academic Research:
AC-IETD-AFC is widely used in academic research institutions to investigate the molecular mechanisms underlying apoptosis and caspase-mediated cell death, contributing to a better understanding of these processes and their implications in various diseases and conditions.
Check Digit Verification of cas no
The CAS Registry Mumber 211990-57-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,1,1,9,9 and 0 respectively; the second part has 2 digits, 5 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 211990-57:
(8*2)+(7*1)+(6*1)+(5*9)+(4*9)+(3*0)+(2*5)+(1*7)=127
127 % 10 = 7
So 211990-57-7 is a valid CAS Registry Number.
211990-57-7Relevant articles and documents
Synthesis, enzymatic evaluation, and docking studies of fluorogenic caspase 8 tetrapeptide substrates
Reszka, Przemyslaw,Schulz, Riad,Methling, Karen,Lalk, Michael,Bednarski, Patrick J.
experimental part, p. 103 - 117 (2010/11/02)
The synthesis, enzymatic evaluation, and molecular modeling studies of new fluorogenic tetrapeptide-based substrates selective for caspase 8, having the general structure Ac-IETD-AXX, are described. Various fluorescent reporter groups (AXX), i.e., 3- and 4-substituted coumarins and quinolin-2(1H)-ones were synthesized by von Pechmann condensation. They were subsequently coupled with the caspase-8-selective tetrapeptide Ac-IETD-OH under newly developed synthetic conditions to give the desired substrates in good yields and in high enantiomeric purity. Based on KM and Vmax values, the new compounds proved to be excellent substrates for recombinant human caspase 8. In contrast, the KM values for the same compounds as substrates for human caspase 3 were approximately 10-20-fold higher. Molecular modeling studies based on the X-ray crystal structures of both human caspases 3 and 8 revealed that there is sufficient room within both active sites to accommodate substrates with moderately bulky substituents in the 3- and 4-positions of the fluorogenic coumarins and quinolin-2(1H)-ones. Automated docking of the substrates into the active sites of both human caspases 3 and 8 with the program Auto-Dock 3 gave structures similar to the published crystallographic structures for the same tetrapeptide bound to caspase 8 in the form of an irreversible inhibitor. The calculated binding energies for the new substrates to either caspase 3 or 8 showed little difference between the substrates, consistent with the K M data. In addition, the calculated binding energies (ΔG) to caspase 8 were considerably more negative than those to caspase 3, also consistent with the KM data. A possible molecular interaction that might explain the selectivity of the IETD tetrapeptide motif for caspase 8 over caspase 3 is discussed.
