UNC926UNC926
MedChemExpress (MCE)
HY-16510
1184136-10-4
99.82%
Powder -20°C 3 years 4°C 2 years In solvent -80°C 2 years -20°C 1 year
Room temperature in continental US
may vary elsewhere.
UNC926 is a methyl-lysine (Kme) reader domain inhibitor that inhibits L3MBTL1 with an IC50 of 3.9 μM.
UNC926 also exhibits a low micromolar affinity for the close homolog, L3MBTL3 ( IC50 of 3.2 μM), with a decrease in affinity for the other MBT domains and no binding to CBX7[1]. UNC926 (1-25 μM) inhibits binding of the 3xMBT domain to H4K20me1.UNC926 inhibits the association of L3MBTL13xMBT with the appropriate histonepeptides in a dose-dependent manner. UNC926 does not have an effect on the binding of 53BP1 to H4K20me1, demonstrating specificity of UNC926 for L3MBTL1 over 53BP1[1].
IC50: 3.9 μM (L3MBTL1), 3.2 μM (L3MBTL3), 15.6 μM (L3MBTL4)[1] In Vitro UNC926 also exhibits a low micromolar affinity for the close homolog, L3MBTL3 ( IC50 of 3.2 μM), with a decrease in affinity for the other MBT domains and no binding to CBX7[1]. UNC926 (1-25 μM) inhibits binding of the 3xMBT domain to H4K20me1.UNC926 inhibits the association of L3MBTL13xMBT with the appropriate histonepeptides in a dose-dependent manner. UNC926 does not have an effect on the binding of 53BP1 to H4K20me1, demonstrating specificity of UNC926 for L3MBTL1 over 53BP1[1]. MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. 0 --> UNC926 Related Antibodies
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[1]. Herold JM, et al. Structure–activity relationships of methyl-lysine reader antagonists. MedChemComm. 2012
3(45):45–51.