MGLL is membrane-associated member of the serine hydrolase superfamily. MGLL functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides. It is most abundantly expressed in skeletal muscle and adipose tissue. Recombinant human MGLL protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.