1. Signaling Pathways
  2. Metabolic Enzyme/Protease
  3. MAGL

MAGL

Monoacylglycerol lipase (MAGL) is a serine hydrolase that plays a crucial role catalysing the hydrolysis of monoglycerides into glycerol and fatty acids. MAGL links the endocannabinoid and eicosanoid systems together by degradation of the abundant endocannabinoid 2-arachidaoylglycerol into arachidonic acid, the precursor of prostaglandins and other inflammatory mediators.

MAGL plays a critical role in lipid signalling: i) it is the major enzyme that controls the levels of 2-AG, an important lipid with various neuroprotective effects; ii) inactivation of MAGL induces an elevation in brain levels of 2-AG and a reduction of AA, a key precursor of pro-inflammatory prostaglandins, resulting in the reduction of neuroinflammation; iii) MAGL regulates the levels of free fatty acids (FFAs) in aggressive cancer cells, and this MAGL-promoted fatty acid network drives a number of pro-tumorigenic signalling pathways. MAGL is emerging as a promising drug target for various diseases.

MAGL Related Products (20):

Cat. No. Product Name Effect Purity
  • HY-15249
    JZL 184 Inhibitor
    JZL 184 is a potent, selective and irreversible MAGL inhibitor that blocks 2-Arachidonoylglycerol (2-AG) hydrolysis in brain membranes (IC50 of 8 nM). JZL 184 displays >300-fold selectivity for MAGL over FAAH.
  • HY-117632
    ABX-1431 Inhibitor 99.96%
    ABX-1431 is a highly potent, selective, and orally available, CNS-penetrant monoacylglycerol lipase (MAGL) inhibitor with an IC50 of 14 nM.
  • HY-114157
    DO-264 Inhibitor 98.81%
    DO-264 is a selective and in vivo-active inhibitor of Abhydrolase Domain Containing 12 (ABHD12), with an IC50 of 11 nM.
  • HY-100337
    WWL70 Inhibitor 99.98%
    WWL70 is a selective alpha/beta hydrolase domain 6 (ABHD6) inhibitor with an IC50 of 70 nM.
  • HY-133130
    JNJ-42226314 Inhibitor 99.59%
    JNJ-42226314 is a competitive, highly selective and reversible non-covalent monoacylglycerol lipase (MAGL) inhibitor. JNJ-42226314 demonstrates dose-dependent enhancement of the major endocannabinoid 2-arachidonoylglycerol (2-AG) as well as efficacy in models of neuropathic and inflammatory pain.
  • HY-111538
    MAGL-IN-1 Inhibitor 99.90%
    MAGL-IN-1 is a potent, selective, reversible and competitive inhibitor of MAGL, with an IC50 of 80 nM. MAGL-IN-1 exhibits anti-proliferative effects against human breast, colorectal, and ovarian cancer cells. MAGL-IN-1 blocks MAGL in cell-based as well as in vivo assays.
  • HY-116141
    7-Hydroxycoumarinyl arachidonate
    7-Hydroxycoumarinyl arachidonate (7-HCA) is a fluorogenic substrate of cytosolic phospholipase A2 (PLA2). 7-Hydroxycoumarinyl arachidonate is also a fluorogenic substrate for monoacylglycerol lipase (MAGL). MAGL protein catalyzes the hydrolysis of 7-Hydroxycoumarinyl arachidonat to generate Arachidonic acid (AA) and the highly fluorescent 7-hydroxyl coumarin (7-HC; HY-N0573). Release of 7-HC can be measured using a fluorometer.
  • HY-136562
    N-Arachidonyl maleimide Inhibitor
    N-Arachidonyl maleimide is a potent, irreversible inhibitor of monoacylglycerol lipase (MAGL) with an IC50 value of 140 nM.
  • HY-15250
    JZL195 Inhibitor 99.75%
    JZL195 is a selective and efficacious dual fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) inhibitor with IC50s of 2 and 4 nM, respectively.
  • HY-18977
    KML29 Inhibitor 99.21%
    KML29 is an extremely selective, orally active and irreversible MAGL inhibitor, with IC50 values of 15 nM, 43 nM and 5.9 nM for mouse, rat and human MAGL, respectively. KML29 exhibits minimal cross-reactivity toward other central and peripheral serine hydrolases, including no detectable activity against FAAH.
  • HY-117474
    MJN110 Inhibitor 99.57%
    MJN110 is an orally active and selective monoacylglycerol lipase (MAGL) inhibitor with IC50s of 9.1 nM and 2.1 nM for hMAGL and 2-arachidonoylglycerol (2-AG), respectively. MJN110 produces opioid-sparing effects and displays strong antihyperalgesic activity.
  • HY-108613
    JJKK 048 Inhibitor ≥98.0%
    JJKK 048 is an ultrapotent and highly selective inhibitor of Monoacylglycerol lipase (MAGL).
  • HY-12332
    JW 642 Inhibitor 99.70%
    JW 642 is a potent inhibitor of monoacylglycerol lipase (MAGL) that displays IC50 values of 7.6, 14, and 3.7 nM for inhibition of MAGL in mouse, rat, and human brain membranes, respectively.
  • HY-114926
    KT185 Inhibitor ≥99.0%
    KT185 is an orally-bioavailable, brain-penetrant and selective ABHD6 inhibitor, with an IC50 0.21 nM in Neuro2A cells.
  • HY-120177
    KT182 Inhibitor ≥99.0%
    KT182 is a potent and selective inhibitor of α/β-hydrolase domain containing 6 (ABHD6), with an IC50 of 0.24 nM in Neuro2A cells.
  • HY-101457
    JZP-430 Inhibitor ≥99.0%
    JZP-430 is a potent, highly selective, irreversible inhibitor of α/β-hydrolase domain 6 (ABHD6) with an IC50 of 44 nM, exhibits ~230-fold selectivity over fatty acid amide hydrolase (FAAH) and lysosomal acid lipase (LAL).
  • HY-120215
    KT203 Inhibitor ≥98.0%
    KT203 is a potent and selective inhibitor of α/β-hydrolase domain containing 6 (ABHD6), with an IC50 of 0.31 nM in Neuro2A cells.
  • HY-N0313
    Euphol Inhibitor 98.82%
    Euphol is a tetracyclic triterpene alcohol isolated from the sap of Euphorbia tirucalli with anti-mutagenic, anti-inflammatory and immunomodulatory effects, orally active. Euphol inhibits the monoacylglycerol lipase (MGL) activity via a reversible mechanism (IC50=315 nM). MGL inhibition in the periphery modulates the endocannabinoid system to block the development of inflammatory pain.
  • HY-111512
    PF-06795071 Inhibitor
    PF-06795071 is a potent and selective covalent MAGL inhibitor with an IC50 of 3 nM.
  • HY-103463
    SA57 Inhibitor ≥99.0%
    SA57 is a potent, selective FAAH inhibitor with IC50s of 3.2 nM and 1.9 nM for mouse and human FAAH. SA57 also inhibits the 2-arachidonoylglycerol hydrolases MAGL (IC50s of 410 nM and 1.4 μM for mouse and human MAGL) and mouse α/β-hydrolase domain-containing protein 6 (mABHD6; IC50 of 850 nM), but not other brain serine hydrolases.
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