Fatty Acid Amide Hydrolase (human, recombinant)

Fatty acid amide hydrolase (FAAH) is a serine hydrolase with a major role in the hydrolysis of endocannabinoids.^1,2,3 It is composed of an N-terminal transmembrane domain, a catalytic domain containing an amidase signature sequence, a polyproline sequence, and a monotopic membrane binding domain.³ FAAH is localized to microsomal and mitochondrial membranes and is highly expressed in the CNS but can also be found in peripheral tissues such as lung, gastrointestinal tract, kidney, liver, bladder, prostate, and testis.^2,4 It primarily catalyzes the inactivation of the endogenous endocannabinoid arachidonoyl ethanolamide (AEA; Item No. 90050) via hydrolysis to arachidonic acid and ethanolamine but has broad substrate selectivity towards fatty acid amides, including oleamide, N-acyltaurines, and other N-acylethanolamines.² Genetic or pharmacologic knockdown of FAAH increases levels of AEA and dampens pain sensitivities and inflammatory endpoints in rodent models of inflammatory pain, allergic contact dermatitis, inflammatory bowel disease, and neuropathic pain.⁵

WARNING This product is not for human or veterinary use.

1. Cravatt, B.F., Giang, D.K., Mayfield, S.P., et al. Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature 384(6604), 83-87 (1996).

2. van Egmond, N., Straub, V.M., and van der Stelt, M. Targeting endocannabinoid signaling: FAAH and MAG lipase inhibitors. Annu. Rev. Pharmacol. Toxicol. 61, 441-463 (2021).

3. Ahn, K., Johnson, D.S., and Cravatt, B.F. Fatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disorders. Expert Opin. Drug Discov. 4(7), 763-784 (2009).

4. Deutsch, D.G., Ueda, N., and Yamamoto, S. The fatty acid amide hydrolase (FAAH). Prostaglandins Leukot. Essent. Fatty Acids 66(2-3), 201-210 (2002).

5. Schlosburg, J.E., Kinsey, S.G., and Lichtman, A.H. Targeting fatty acid amide hydrolase (FAAH) to treat pain and inflammation. AAPS J. 11(1), 39-44 (2009).

Butler, C.R., Beck, E.M., Harris, A.R., et al. Azetidine and piperidine carbamates as efficient, covalent inhibitors of monoacylglycerol lipase. J. Med. Chem. 60(23), 9860-9873 (2017).