Antigen: human monoacylglycerol lipase amino acids 1-14 · Host: rabbit · Application(s): IHC and WB · Endocannabinoids, such as arachidonoyl ethanolamide (AEA) and 2-Arachidonoyl glycerol (2-AG), function as short-range modulators of cell and synaptic activity. Monoacylglycerol lipase (MAGL) hydrolyzes 2-AG to terminate its biological actions ¹ and works consecutively with hormone-sensitive lipase (HSL) to mobilize fatty acids from the triglyceride stores of adipocytes.² MAGL has a molecular weight of ~33 kDa and exhibits a high degree of homology among human, mouse, and rat at the amino acid level.^3,4,1,2 The enzyme is expressed in a variety of tissues with most abundant expression in skeletal muscle and adipose tissue, suggesting a role of MAGL in monoglyceride hydrolysis in diverse tissues. Cayman Chemical’s MAGL polyclonal antibody can be used for western blot and immunohistochemical (formalin-fixed paraffin-embedded tissue) analysis for MAGL on samples of human, mouse, rat, and bovine origin. Other applications for use of this antibody have not yet been tested.

1 Dinh, T.P., Carpenter, D., Leslie, F.M., et al. Brain monoglyceride lipase participating in endocannabinoid inactivation. Proc Natl Acad Sci USA 99(16) 10819-10824 (2002).

2 Karlsson, M., Reue, K., Xia, Y., et al. Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene. Gene 272 11-18 (2001).

3 Karlsson, M., Contreras, J.A., Hellman, U., et al. cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases. J Biol Chem 272 27218-27223 (1997).

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