Related Experiment Video
Updated: Aug 27, 2025

Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening
Published on: May 13, 2020
Fluorimetric Assay of FAAH Activity
Clotilde B Angelucci1, Roberto Giacominelli-Stuffler2, Mauro Maccarrone3,4
1Faculty of Veterinary Medicine, University of Teramo, Teramo, Italy. bcangelucci@unite.it.
Abstract:
Fatty acid amide hydrolase (FAAH) is the enzyme responsible for the degradation of anandamide (N-arachidonoylethanolamine, AEA) to arachidonic acid (AA) and ethanolamine. The method described here measures FAAH activity through the fluorometric arachidonoyl-7-amino-4-methyl-coumarin amide (AAMCA) substrate, which allows a simple and sensitive assay suitable for high-throughput screening tests. FAAH catalyzes the hydrolysis of AAMCA producing AA and the highly fluorescent compound 7-amino-4-methylcoumarin (AMC).
More Related Videos
10:21Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
06:54A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
Published on: June 3, 2021