Date published: 2025-9-12

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ZNF584 Inhibitors

Chemical inhibitors of ZNF584 include a variety of compounds that target different cellular pathways, each with a unique mechanism to inhibit the function of this protein. Palbociclib, a CDK4/6 inhibitor, prevents the phosphorylation of proteins that are crucial for the DNA-binding activity of ZNF584, thus directly interfering with its ability to regulate gene expression. Trichostatin A, an HDAC inhibitor, alters the acetylation status of histones surrounding the DNA, which can change the accessibility of the DNA binding sites for ZNF584, thereby inhibiting its function. This is complemented by the action of MG-132, a proteasome inhibitor, which can stabilize regulatory proteins that repress the activity of ZNF584 by preventing their degradation.

Further inhibition is achieved through the use of LY294002 and Wortmannin, both PI3K inhibitors, which disrupt the PI3K/AKT pathway that is potentially involved in post-translational modifications of proteins that associate with ZNF584. Rapamycin, an mTOR inhibitor, contributes to this inhibition by disturbing downstream signaling pathways that influence protein synthesis and degradation, which can indirectly inhibit ZNF584. Staurosporine broadly targets kinases that may phosphorylate proteins interacting with ZNF584, hence impacting its function. U0126 and SB203580, inhibitors of MEK and p38 MAPK, respectively, prevent the activation of pathways that could lead to the phosphorylation of ZNF584-associated proteins, while SP600125, a JNK inhibitor, blocks the phosphorylation of substrates that may modify ZNF584's activity. Y-27632, a ROCK inhibitor, disrupts cellular mechanics, which can influence ZNF584's localization and function. Lastly, Alsterpaullone, another cyclin-dependent kinase inhibitor, joins the array of inhibitors by also preventing the phosphorylation of proteins essential for ZNF584's activity, thereby directly inhibiting the protein's functional capabilities.

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