LEI-106, a novel potent sn-1 DAGLalpha inhibitor, blocks the hydrolysis of sn-1-oleoyl-2-AG, inhibits the hydrolysis of 2-AG by the monoacylglycerol lipase ABHD6.
(R)-KT109 is the (R) isomer of the diacylglycerol lipase β (DAGLβ) inhibitor KT109 . (R)-KT109 is an inhibitor of DAGLβ (IC50 = 0.79 nM) and of DAGLα-mediated hydrolysis of 1-stearoyl-2-arachidonoyl-sn-glycerol . It also inhibits α β-hydrolase domain-containing protein 6 (ABHD6) with an IC50 value of 2.51 nM. (R)-KT109 is more potent at DAGLβ, DAGLα, and ABHD6 than (S)-KT109 .
JJH260 is an N-hydroxy hydantoin carbamate that inhibits androgen-induced gene 1 (AIG1), an enzyme that hydrolyzes fatty acid esters of hydroxy fatty acids (FAHFAs). It blocks the hydrolysis of 9-PAHSA with an IC50 value of 0.57 μM. JJH260 also inhibits the novel FAHFA hydrolase androgen-dependent TFPI-regulating protein (ADTRP; IC50 = 8.5 μM), as well as the serine hydrolase ABHD6 and the lysophospholipases LYPLA1 and LYPLA2. JJH260 inhibits the FAHFA hydrolase activity of LNCaP and T cell lysates and intact cells.
(S)-KT109 is the (S) isomer of the diacylglycerol lipase β (DAGLβ) inhibitor KT109 . (S)-KT109 is a less potent inhibitor of DAGLβ (IC50 = 39.81 nM), DAGLα-mediated hydrolysis of 1-stearoyl-2-arachidonoyl-sn-glycerol (IC50 = 794.3 nM), and α β-hydrolase domain-containing protein 6 (ABHD6; IC50 = 630.9 nM) than (R)-KT109 .
ABC34 is an inactive control probe for JJH260 , the inhibitor of androgen-induced gene 1 (AIG1), an enzyme that hydrolyzes fatty acid esters of hydroxy fatty acids (FAHFAs). ABC34 demonstrates an IC50 value greater than 25 μM for the inhibition of 9-PAHSA but is more potent in blocking the serine hydrolase ABHD6 and the palmitoyl-protein hydrolase PPT1, which are both off-targets of JJH260.
FP-biotin is a potent organophosphorus toxicant, ideal for identifying novel biomarkers of organophosphorus toxicant exposure. It measures FAAH, ABHD6, and MAG-lipase activity, specifically in plasma studies, due to the efficient purification of biotinylated peptides through binding to immobilized avidin beads.