Monoacylglycerol Lipase (human, recombinant)

Endocannabinoids such as 2-arachidonoyl glycerol (2-AG; Item No. 62160) and arachidonyl ethanolamide (AEA; Item No. 90050) 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.^1,2 MAGL is the principal 2-AG hydrolase in the mammalian brain accounting for greater than 80% of the total 2-AG hydrolase activity.³ Human recombinant MAGL was characterized using 4-nitrophenylacetate as a substrate, which upon hydrolysis by MAGL, froms 4-nitrophenol with an absorbance maximum at 412 nm.

WARNING This product is not for human or veterinary use.

1. Dinh, T.P., Freund, T.F., and Piomelli, D. A role for monoglyceride lipase in 2-arachidonoylglycerol inactivation. Chem. Phys. Lipids 121(1-2), 149-158 (2002).

2. Vila, A., Rosengarth, A., Piomelli, D., et al. Hydrolysis of prostaglandin glycerol esters by the endocannabinoid-hydrolyzing enzymes, monoacylglycerol lipase and fatty acid amide hydrolase. Biochemistry 46(33), 9578-9585 (2007).

3. Blankman, J.L., Simon, G.M., and Cravatt, B.F. A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol. Chem. Biol. 14(12), 1347-1356 (2007).