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Fatty acid amide hydrolase (FAAH), belonging to an amidase-signature (AS) protein family, is a membrane-bound protein predominantly in microsomal and mitochondrial fractions that catalyzes the hydrolysis of several bioactive lipids, including anandamide, 2-arachidonoylglycerol (2-AG) and oleamide. The mammalian FAAHs are 63 kDa (579 amino acids in length) proteins characterized by containing several domains defined by homology and function, including, a highly conserved seine-and-glycine-rich AS domain, a predicted transmembrane domain and a proline rich domain. Results of mutation studies suggest, unlike other members of AS protein family, the catalytic activity of FAAH is not associated with the Ser-His-Asp triad but possibly with Ser217 and Lys142.

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  7. A3714 PF-04457845 PF-04457845 is a potent and exquisitely selective inhibitor of the enzyme fatty acid amide hydrolase (FAAH), with an IC50 of 7.2nM, and both analgesic and antiinflammatory effects in animal studies comparable to naproxen.
  8. A3571 LY2183240 LY2183240 is a novel and highly potent blocker of anandamide uptake (IC50 = 270 pM). LY2183240 inhibits fatty acid amide hydrolase (FAAH) activity (IC50 = 12.4 nM).
  9. A4372 URB597 URB597, also known as KDS-4103, is a potent and selective inhibitor of fatty-acid amide hydrolase (FAAH), an enzyme catalyzing the intracellular hydrolysis of the endocannabinoid anandamide, with values of 50% inhibition concentration IC50 of 5 nM and 3 nM in rat brain membranes and human liver microsomes respectively.
  10. A4361 JNJ-1661010 JNJ-1661010, a piperazinyl phenyl urea with its structure distinct from alkylcarbamic acid esters and α–ketoheterocyclic compounds, is a potent and selective inhibitor of fatty acid amide hydrolase (FAAH) that covalently binds to the active site of FAAH through cleavage of the urea functionality generating aniline and a FAAH-poperazinyl carbamate.
  11. C5719 Oleyl Trifluoromethyl Ketone

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