The enzyme fatty acid amide hydrolase (FAAH) is capable of hydrolyzing and inactivating anandamide (AEA) and other fatty acid amides that act as agonists for the central cannabinoid (CB1) receptor.1 CAY10570 is a reversible competitive inhibitor of FAAH activity exhibiting an IC50 value of 1.3 µM.2 CAY10570 has no affinity for the human CB1 receptor and acts as a competitive inhibitor of FAAH activity without being hydrolyzed by the enzyme.2
1
Cravatt, B.F., Giang, D.K., Mayfield, S.P., et al. Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature38483-87(1996).
2
Muccioli, G.G., Fazio, N., Scriba, G.K.E., et al. Substituted 2-thioxoimidazolidin-4-ones and imidazolidine-2,4-diones as fatty acid amide hydrolase inhibitors templates. J Med Chem49417-425(2006).
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CCCCCCCCCCN1C(=S)NC(c2ccccc2)(c2ccccc2)C1=O
Background Reading
Muccioli, G.G., Fazio, N., Scriba, G.K.E., et al. Substituted 2-thioxoimidazolidin-4-ones and imidazolidine-2,4-diones as fatty acid amide hydrolase inhibitors templates. J Med Chem49417-425(2006).
Cravatt, B.F., Giang, D.K., Mayfield, S.P., et al. Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature38483-87(1996).
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