Date published: 2025-9-18

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ZNF10 Inhibitors

Chemical inhibitors of ZNF10 can function through various modes of action, primarily by targeting the protein kinase C (PKC) pathway, which is instrumental in the phosphorylation of ZNF10. Phorbol 12-myristate 13-acetate (PMA) is known to activate PKC, leading to the phosphorylation of ZNF10, which affects its DNA-binding capability and thus functionally inhibits it. Conversely, compounds like Staurosporine and Chelerythrine Chloride act as PKC inhibitors, preventing the phosphorylation of ZNF10, which is essential for its role as a transcription factor. Similarly, Bisindolylmaleimide I, Gö 6983, and Ro-31-8220, all inhibit PKC, thereby reducing ZNF10's ability to bind to DNA and regulate gene expression.

Further down this inhibitory cascade, Ruboxistaurin and Enzastaurin selectively inhibit PKCβ, a specific isoform of PKC that, when active, phosphorylates ZNF10. This phosphorylation is crucial for ZNF10's regulatory functions, and inhibition of PKCβ results in a decrease in ZNF10 activity. Sotrastaurin, another PKC inhibitor, prevents the phosphorylation of ZNF10, indirectly leading to its inhibition. K-252a, with its high affinity for PKC, inhibits the kinase's activity and thus the functional activity of ZNF10. Lastly, Hispidin inhibits PKC, which is necessary for phosphorylation of ZNF10, leading to the inhibition of its transcription factor activity. Each of these inhibitors targets the PKC-related phosphorylation process, which is essential for the proper functioning of ZNF10, and by obstructing this pathway, they effectively inhibit the activity of ZNF10.

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