MGLL Human

Monoglyceride Lipase is responsible for the hydrolysis of monoacylglycerides into free fatty acids and glycerol . This reaction is essential for the regulation of lipid signaling molecules and energy homeostasis. The enzyme is composed of 303 amino acids and has a molecular mass of approximately 34 kDa . It is typically expressed in various tissues, including the brain, liver, and adipose tissue.

Recombinant Human Monoglyceride Lipase is produced using E. coli expression systems . The recombinant protein is often tagged with a 6-His tag for purification purposes. The production process involves cloning the human MGLL gene into an expression vector, transforming the vector into E. coli cells, and inducing protein expression. The recombinant protein is then purified using affinity chromatography techniques.

Recombinant Monoglyceride Lipase is widely used in biochemical research to study lipid metabolism and signaling pathways. It is also utilized in drug discovery and development, particularly in the context of diseases related to lipid metabolism, such as obesity, diabetes, and neurodegenerative disorders .

Monoglyceride Lipase plays a significant role in the breakdown of the endocannabinoid 2-arachidonoylglycerol (2-AG), which is involved in various physiological processes, including pain sensation, appetite regulation, and immune response . Inhibition of MGLL has been shown to have therapeutic potential in conditions such as Alzheimer’s disease, where it can reduce the accumulation of β-amyloid and decrease the expression of β-site amyloid precursor protein cleaving enzyme 1 (BACE1) .

Recombinant Human Monoglyceride Lipase is typically supplied as a filtered solution in Tris, NaCl, Brij-35, and EDTA . It should be stored at -70°C to maintain its stability and activity. It is important to avoid repeated freeze-thaw cycles to prevent protein degradation.