1416133-88-4

Endocannabinoids such as 2-arachidonoyl glycerol (2-AG) and arachidonoyl ethanolamide are biologically active lipids that are involved in a number of synaptic processes including activation of cannabinoid receptors. Monoacylglycerol lipase (MAGL) is a serine hydrolase responsible for the hydrolysis of 2-AG to arachidonic acid and glycerol, thus terminating its biological function. JW 618 is an inhibitor of MAGL that displays IC₅₀ values of 123, 385, and 6.9 nM for inhibition of MAGL in mouse, rat, and human brain membranes, respectively.¹ JW 618 is selective for MAGL, requiring much higher concentrations to effectively inhibit fatty acid amide hydrolase activity (IC₅₀s all > 50 μM for mouse, rat, and human brain membranes).¹

1. Chang, J.W., Niphakis, M.J., Lum, K.M., et al. Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates Chem. Biol. 19(5),579-588(2012).