JQ1-S(GlcNAc)Cq

JQ1-S(GlcNAc)cQ inhibits CRBN binding in a cell-free TR-FRET assay with an IC₅₀ of 1.2 μM, showing a 13-fold lower affinity than its parent compound JQ1-ScQ^[1].
JQ1-S(GlcNAc)cQ strongly suppresses CRBN-BRD4(BD1) ternary complex formation in a cell-free TR-FRET assay^[1].
JQ1-S(GlcNAc)cQ strongly suppresses CRBN-BRD4(BD2) ternary complex formation in a cell-free TR-FRET assay^[1].
JQ1-S(GlcNAc)cQ is a specific substrate for wild-type hOGA in a cell-free assay, undergoing efficient deglycosylation to JQ1-ScQ with a k_cat of 0.28 s⁻¹ and K_m of 49.8 μM, while inactive hOGA^D174N does not catalyze deglycosylation^[1].
JQ1-S(GlcNAc)cQ (10 μM; 0-24 h) induces BRD4(BD1)-EGFP degradation in HEK293T reporter cells, which is partially rescued by hOGA inhibition with TMG and proceeds with rapid initial degradation within 1 h at 10 μM^[1].
JQ1-S(GlcNAc)cQ (10 μM; 0-24 h) induces BRD4(BD2)-EGFP degradation in HEK293T reporter cells, which is partially rescued by hOGA inhibition with TMG and proceeds with rapid initial degradation within 1 h at 10 μM^[1].
JQ1-S(GlcNAc)cQ (5 μM; 2-12 h) induces rapid degradation of endogenous BRD4 in HEK293T cells, and this degradation is dependent on proteasome and Cullin-RING ligase activity, as well as BRD4 and CRBN binding^[1].
JQ1-S(GlcNAc)cQ (0-10 μM; 12 h) degrades endogenous BRD4 in HEK293T cells with a DC₅₀ of 2.1 μM, and overexpression of hOGA enhances its potency to a DC₅₀ of 0.1 μM, matching the activity of JQ1-ScQ^[1].

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