LEI105

LEI105 (1 µM; 30 min) inhibits DAGLb hydrolase activity by 51% in human term placental membrane lysates^[1].
LEI105 inhibits recombinant human DAGL-α-mediated natural substrate conversion in a fluorescence-based assay with a pIC₅₀ of 7.9^[2].
LEI105 inhibits recombinant human DAGL-α in a radiometric assay with a pIC₅₀ of 6.6^[2].
LEI105 inhibits endogenous DAGL-α activity in mouse brain membrane proteome with a pIC₅₀ of 7.5, as measured by competitive ABPP^[2].
LEI105 inhibits recombinant human DAGL-β activity in transfected HEK293T cell membranes with a pIC₅₀ of 7.4, as measured by competitive ABPP^[2].
LEI105 potently inhibits recombinant human DAGL-β in a colorimetric assay with a pIC₅₀ of 8.1^[2].
LEI105 inhibits endogenous DAGL-β activity in mouse spleen membrane proteome, as measured by competitive ABPP^[2].
LEI105 (10 μM) is highly selective for DAGLs over other serine hydrolases including FAAH in mouse brain proteome, as it does not inhibit TAMRA-FP labeling of off-target enzymes at 10 μM^[2].
LEI105 (10 μM; 30 min) is highly selective for DAGL-α over other serine hydrolases in mouse brain proteome, as only DAGL-α labeling is reduced by more than 20% at 10 μM for 30 min^[2].
LEI105 does not significantly interact with the cannabinoid CB₁ receptor, with a pK_i value below 5^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.