|Other Names||Fatty-acid amide hydrolase 2, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2, AMDD|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.|
|Cellular Location||Membrane; Single-pass membrane protein|
|Tissue Location||Highly expressed in the brain, small intestine and testis. Also expressed in the heart, kidney, liver, lung and prostate.|
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Provided below are standard protocols that you may find useful for product applications.
FAAH2 encodes a fatty acid amide hydrolase that shares a conserved protein motif with the amidase signature family of enzymes. The encoded enzyme is able to catalyze the hydrolysis of a broad range of bioactive lipids, including those from the three main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. This enzyme has a preference for monounsaturated acyl chains as a substrate.
Kaczocha, M., et al. J. Biol. Chem. 285(4):2796-2806(2010)Karbarz, M.J., et al. Anesth. Analg. 108(1):316-329(2009)Wei, B.Q., et al. J. Biol. Chem. 281(48):36569-36578(2006)
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