Fatty Acid Amide Hydrolase (FAAH) Activity Assay Kit (Fluorometric)

MILPITAS, Calif. - Sept. 19, 2018 - PRLog -- Fatty Acid Amide Hydrolase (FAAH; EC: 3.5.1.99, Oleamide Hydrolase, Anandamide Amidohydrolase) is a mammalian integral membrane enzyme, and is a key regulator in lipid signaling. FAAH degrades naturally occurring fatty acid amides such as cannabinoid anandamide and oleamide, a sleep-inducing substance. In general, fatty acid amides are endogenous lipid ligands which activate the cannabinoid (CB) G-protein coupled receptors CB1 and CB2. CB1 and CB2 modulate physiological and behavioral processes such as pain, and anti-inflammation. Therefore, FAAH is crucial in the termination of fatty acid amide bioactive functions. Recent studies showed that blockage of FAAH activity led to increased fatty acid amides levels in nervous system and peripheral tissues. Thus, the study of FAAH and its potential inhibitors could develop novel treatment strategies for pain and central nervous system disorders due to the analgesic, anxiolytic and anti-inflammatory properties that are observed when elevated fatty acid amides are present in humans.

In BioVision's FAAH Assay Kit, FAAH hydrolyzes a non-fluorescent substrate releasing 7-amino-4-methylcoumarin (AMC), a fluorophore, which can be easily measured at Ex/Em= 360/465 nm. The kit provides a specific inhibitor that can be used to compensate for potential non-specfic background in unknown samples. The stable fluorescence signal is positively correlated to FAAH enzymatic activity in samples. The kit offers a rapid, simple, sensitive, reproducible assay and is suitable for detecting FAAH activity as low as 0.1 µU.

Figure:  FAAH specific activity of two rat liver microsome preparations (RLM1 and RLM2) and rat liver lysate (RLL: 80 µg). Assays were performed following the kit protocol.

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