Monoacylglycerol Lipase (human, recombinant)

Endocannabinoids such as 2-arachidonoyl glycerol (2-AG, Cay-62160) and arachidonyl ethanolamide (AEA, Cay-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. MAGL is the principal 2-AG hydrolase in the mammalian brain accounting for greater than 80% of the total 2-AG hydrolase activity. 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.Synonyms: MAGL, MGL. Purity: >90% estimated by SDS-PAGE. Source: Active human recombinant C-terminal His-tagged protein expressed in E. coli. Amino Acids: 2-313 (full length). MW: 39 kDa. Storage Buffer: 50 mM HEPES, pH 7.4, with 100 mM sodium chloride, 5 mM MgCl2, 0.1% CHAPS, and 25% glycerol. UniProt Accession #: Q99685.