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Antigen:
human monoacylglycerol lipase amino acids 1-14
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Host:
rabbit
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Application(s):
WB and IHC
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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.
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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., Piomelli, D. A role for monoglyceride lipase in 2-arachidonoylglycerol inactivation. Chem Phys Lipids 121 149-158 (2002).
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