M12

M12 (20 μM; 6 h) reduces DDX18 protein levels in Jurkat cells, and quantitative whole-proteome analysis reveals a decrease in DDX18 protein abundance^[1].
M12 (0-25 μM; 18 h) reduces DDX18 protein levels in MOLT4 cells in a dose-dependent manner^[1].
M12 (20 μM; 18 h) reduces DDX18 protein levels without altering DDX18 mRNA levels in Jurkat cells^[1].
M12 (20 μM; 18 h) induces the degradation of DDX18 in Jurkat cells; pretreatment with MLN7243 (HY-100487) (0.5 μM), MLN4924 (HY-70062) (1 μM), or MG132 (HY-13259) (5 μM) for 1 h rescues DDX18 degradation, supporting that this process depends on the ubiquitin-proteasome system^[1].
Following treatment with M12 (20 μM; 18 h), the mRNA abundance of DDX18 in Jurkat cells remains unchanged, indicating that M12-induced DDX18 reduction occurs exclusively at the protein level^[1].
M12 (0-25 μM; 18 h) induces DDX18 degradation in wild-type Jurkat cells, whereas DCAF11 knockout blocks M12-induced DDX18 degradation^[1].
M12 induces DCAF11-DDX18 proximity in the TR-FRET assay with cell lysate, with an EC₅₀ of 1.76 μM; in plain buffer, M12 alone fails to induce the proximity of the two proteins, and boiled lysate also cannot support this effect^[1].
M12 induces DCAF11-DDX18 proximity in the presence of GST (0.5 mg/mL) and GSH (0.2 mg/mL), with an EC₅₀ of 385 nM; no equivalent proximity-inducing effect is observed in the absence of GST/GSH^[1].
Incubation of M12 (1 μM; 30 min; room temperature) with GST (0.5 mg/mL) and reduced GSH (0.2 mg/mL) results in the formation of GSH-M12, indicating that GST mediates the glutathionylation of M12^[1].
M12 (10 μM; 1 h) produces a metabolite with a mass consistent with that of GSH-M12 in cell-derived samples, supporting the conversion of M12 to a glutathionylated active species in the cellular environment^[1].

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