Oleoylethanolamide (OEA) 98%+ – Powder, 5 grams

OEA binds directly to and activates peroxisome proliferator-activated receptor alpha (PPAR-alpha), a ligand-activated nuclear transcription factor that, upon activation, heterodimerizes with retinoid X receptor (RXR) and binds PPAR-response elements in target gene promoters to upregulate fatty acid oxidation and lipid metabolism genes. Cell-based PPAR-alpha transactivation reporter assays, using a PPAR-response-element-driven luciferase construct, are the standard method for confirming and quantifying OEA's agonist activity at this receptor relative to synthetic PPAR-alpha agonist reference compounds (such as fenofibrate).

OEA is synthesized via hydrolysis of N-acylphosphatidylethanolamine (the same precursor class that generates other N-acylethanolamines, including the endocannabinoid anandamide) and is degraded by fatty acid amide hydrolase (FAAH), the same enzyme that degrades anandamide. This shared biosynthetic and degradative machinery means that FAAH inhibitor compounds, used in endocannabinoid research, also affect OEA levels — a consideration relevant to experimental design when FAAH inhibitors are used and PPAR-alpha-mediated effects need to be distinguished from cannabinoid-receptor-mediated effects.

Standard FAAH activity assays measure the enzymatic hydrolysis rate of OEA (or a fluorogenic/radiolabeled substrate analog) into oleic acid and ethanolamine, typically using tissue homogenates, recombinant FAAH enzyme preparations, or cell lysates. These assays allow researchers to characterise FAAH kinetic parameters (Km, Vmax) with OEA as substrate and to evaluate the potency of FAAH inhibitor compounds, which indirectly elevate OEA tissue concentration by blocking its primary degradation pathway.