FAAH Background Information FAAH is a membrane-bound enzyme fatty acid amide hydrolase, responsible for the hydrolysis of multiple primary and secondary fatty acid amides, including the neuromodulatory compounds anandamine and oleamide (1). The degradation of anandamide to arachadonic acid and oleamide to oleic acid, terminates the signaling function of these molecules (2, 3). FAAH degrades amides and esters with equivalent catalytic efficiency, enabling FAAH to function effectively as both an amidase and esterase (4). FAAH contributes to anandamide uptake by creating and maintaining an inward concentration gradient for anandamide (5). A natural single nucleotide polymorphism mutation in human FAAH in its homozygous form is strongly associated with problem drug use (6). This results in a missense mutation (385C-->A) that converts a conserved proline residue to threonine (Pro129-->Thr), producing an FAAH variant that displays normal catalytic properties but enhanced sensitivity to proteolytic degradation (6). Genetic mutations in FAAH consitute an important risk factor for problem drug use (6). The human FAAH gene maps to chromosome 1p33 (7).
FAAH (27-Y)
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FAAH (27-Y): sc-100739. Western blot analysis of FAAH expression in non-transfected: sc-117752 (A) and mouse FAAH transfected: sc-125319 (B) 293T whole cell lysates.
FAAH (27-Y): sc-100739. Western blot analysis of FAAH expression in A-431 whole cell lysate.
FAAH (27-Y): sc-100739. Western blot analysis of FAAH expression in non-transfected: sc-117752 (A) and human FAAH transfected: sc-112472 (B) 293T whole cell lysates.
FAAH (27-Y): sc-100739. Western blot analysis of FAAH expression in non-transfected: sc-117752 (A) and mouse FAAH transfected: sc-125318 (B) 293T whole cell lysates.