Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Lipid Composition Drives Mutant Huntingtin Dimerization and Membrane Association: Insights from Computational Simulations.

Molecules (Basel, Switzerland)·2026
Same author

Targeting GPR18: Structural modelling, ligand discovery, and therapeutic potential in neuroinflammatory disorders.

Biochemical pharmacology·2026
Same author

Sustained Palmitoylethanolamide Infusion Restores Incentive Motivation and Synaptic Plasticity in the Tg2576 Mouse Model of Alzheimer's Disease.

Cells·2026
Same author

Functional validation of the novel KIF5A p.R17Q VUS reveals defective axonal transport in iPSC-motoneurons from a SPG10 patient.

Frontiers in genetics·2026
Same author

Unraveling Endocannabinoid Signaling Pathways in Cisplatin-Induced Ototoxicity.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2026
Same author

Bone inflammation in postmenopausal women with type 2 diabetes or obesity in relation to Wnt signaling and bone strength.

Metabolism: clinical and experimental·2026

Related Experiment Video

Updated: Mar 20, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

25.0K

Assay of FAAH Activity.

Monica Bari1, Monica Feole2, Mauro Maccarrone2,3

  • 1Department of Experimental Medicine and Surgery, Tor Vergata University of Rome, Rome, Italy. Bari@med.uniroma2.it.

Methods in Molecular Biology (Clifton, N.J.)
|June 2, 2016
PubMed
Summary

Fatty acid amide hydrolase (FAAH) enzyme activity is measured by quantifying radioactive products from anandamide (AEA) hydrolysis. This method quantifies ethanolamine, indicating FAAH enzyme function.

Keywords:
AEAArachidonic acidBioactive lipidsEndocannabinoidsEnzymeEthanolamineFAAH

More Related Videos

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
11:01

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase

Published on: November 23, 2016

10.3K
Author Spotlight: High-Sensitivity Tissue Factor Activity Assay for Plasma Diagnosis
03:53

Author Spotlight: High-Sensitivity Tissue Factor Activity Assay for Plasma Diagnosis

Published on: December 29, 2023

1.3K

Related Experiment Videos

Last Updated: Mar 20, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

25.0K
Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
11:01

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase

Published on: November 23, 2016

10.3K
Author Spotlight: High-Sensitivity Tissue Factor Activity Assay for Plasma Diagnosis
03:53

Author Spotlight: High-Sensitivity Tissue Factor Activity Assay for Plasma Diagnosis

Published on: December 29, 2023

1.3K

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Fatty acid amide hydrolase (FAAH) is a key intracellular enzyme.
  • FAAH hydrolyzes endogenous anandamide (AEA), a lipid mediator, terminating its biological effects.
  • The hydrolysis products are arachidonic acid and ethanolamine.

Purpose of the Study:

  • To describe a method for measuring FAAH activity.
  • To quantify the products of AEA hydrolysis catalyzed by FAAH.

Main Methods:

  • Utilizes a radioactive substrate, specifically [(14)C-ethanolamine]-AEA.
  • Measures FAAH activity by quantifying the radioactive product, [(14)C]-ethanolamine.

Main Results:

  • The described method allows for the quantification of FAAH activity.
  • Radioactive labeling enables sensitive detection of hydrolysis products.

Conclusions:

  • This method provides a reliable way to assess FAAH enzyme activity.
  • Understanding FAAH function is crucial for research into lipid mediator signaling pathways.