MGLL Human, Active

MAGL is a member of the serine hydrolase superfamily and contains the GXSXG consensus motif common to most serine hydrolases. It harbors a catalytic triad composed of serine, aspartate, and histidine residues (Ser122-Asp239-His269 in human MAGL) . The enzyme’s structure includes a canonical α/β-hydrolase fold characterized by a central β-sheet surrounded by six α-helices. Additionally, α-helices α4, α5, and α6 form a U-shaped cap domain that likely opens upon interfacial activation, allowing substrates to access the enzyme’s active site .

MAGL is primarily involved in the deactivation of the endocannabinoid 2-arachidonoylglycerol (2-AG), which is the most abundant endogenous lipid agonist for cannabinoid receptors in the brain and other parts of the body . In the central nervous system, MAGL is localized to presynaptic nerve terminals of both excitatory and inhibitory synapses, where it regulates the actions of 2-AG on synaptic transmission and plasticity .

Recombinant human MAGL is produced using genetic engineering techniques, where the human gene encoding MAGL is inserted into a host organism, such as Escherichia coli (E. coli), to produce the enzyme in large quantities . This recombinant enzyme is often tagged with a His-tag at the C-terminal to facilitate purification and is characterized by its high purity and activity .

Recombinant human MAGL is widely used in research to study lipid metabolism, endocannabinoid signaling, and the role of MAGL in various physiological and pathological processes . It is also used in enzyme activity assays, inhibitor screening, and structural studies .

The recombinant human MAGL enzyme is typically stored at -80°C and is stable for at least two years under these conditions . It is shipped on dry ice to maintain its stability during transport .