Date published: 2025-9-21

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ZFP386 Inhibitors

Chemical inhibitors of ZFP386 can exert their inhibitory effects through various mechanisms related to the signaling pathways and cellular processes that ZFP386 is involved in. Palbociclib, for instance, selectively inhibits cyclin-dependent kinases CDK4 and CDK6. This inhibition can lead to reduced phosphorylation of proteins that interact with ZFP386, which in turn can impair the functional activity of ZFP386. Trichostatin A, as a histone deacetylase inhibitor, can alter chromatin structure and potentially impede the DNA-binding activity of ZFP386, leading to its functional inhibition. Similarly, the proteasome inhibitor MG-132 can prevent the degradation of natural inhibitors of ZFP386, resulting in an increase in their levels and subsequent inhibition of ZFP386's activity.

LY294002 and Wortmannin are both inhibitors of PI3K and can interfere with the AKT signaling pathway. This disruption can impair the phosphorylation states of ZFP386 or its cofactors, inhibiting ZFP386's activity. PD 98059 and SB203580, inhibitors of MEK and p38 MAPK respectively, can disrupt the MAPK/ERK pathway, which is often crucial for the phosphorylation and function of ZFP386 or proteins that regulate ZFP386. Rapamycin, an mTOR inhibitor, can disrupt phosphorylation and activation of proteins that regulate ZFP386, leading to its functional inhibition. PP2, a Src family kinase inhibitor, can inhibit signaling pathways that activate ZFP386, while SP600125, a JNK inhibitor, can interfere with the phosphorylation state of ZFP386 or its associated factors, leading to the inhibition of ZFP386's activity. BAY 11-7082 targets NF-κB activation, which, when inhibited, can reduce the interaction of this transcription factor with ZFP386, thereby inhibiting its function. Lastly, Y-27632, which inhibits ROCK, can affect the actin cytoskeleton and potentially interfere with the cellular localization or functional expression of ZFP386, culminating in its inhibition. Through these diverse yet specific mechanisms, the activity of ZFP386 can be effectively inhibited by these chemical compounds.

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