RAJQ14

RAJQ14 (10 μM) selectively binds to the bromodomains of BRD2, BRD3, and BRD4, increasing their thermal stability^[1].
RAJQ14 (10 μM; 2 h) binds to both RPN13 and BRD4 in live HEK293T cells^[1].
RAJQ14 (0.1-2.5 μM; 2-24 h) induces dose-dependent and time-dependent degradation of BRD4 in HEK293T cells^[1].
RAJQ14 (1 μM; 6 h) selectively induces degradation of BRD2, BRD3, and BRD4 in HEK293T cells, with no off-target degradation of other bromodomain-containing proteins^[1].
RAJQ14 (0.1-2.5 μM; 24 h) induces BRD4 degradation in CRBN-knockout HEK293T cells that is independent of the E3 ligase CRBN^[1].
RAJQ14 (1-100 μM; overnight) binds to multiple 19S proteasome cap subunits (including RPN1, RPN10, RPN13, and USP14) and BET proteins (BRD2, BRD3, BRD4) in HCT116 cells, independent of RPN13 expression^[1].
RAJQ14 (0.1-2.5 μM; 24 h) induces BRD4 degradation in RPN13-knockou HCT116 cells independent of RPN13, likely via engagement of alternative 19S proteasome cap subunits^[1].
RAJQ14 (0.1-2.5 μM; 24 h) induces BRD4 degradation in T47D-shRPN1-Dox cells that is not fully dependent on RPN1, as compensatory upregulation of RPN13 and RPN11 maintains degrader activity^[1].
RAJQ14 (2.5 μM; 6 h) induces BRD4 degradation in HEK293T cells via a ubiquitination-independent mechanism, as BRD4 ubiquitination is not detected during degradation^[1].

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