Date published: 2025-10-12

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ZNF323 Inhibitors

Chemical inhibitors of ZNF323 encompass a range of compounds that interfere with various cellular signaling pathways and molecular processes which are integral to the protein's function. Staurosporine and Bisindolylmaleimide I target Protein Kinase C (PKC), a key enzyme that regulates protein phosphorylation. By inhibiting PKC, these chemicals reduce phosphorylation levels within the cell, thereby decreasing ZNF323 activity, as phosphorylation is a post-translational modification that can influence ZNF323's function. Similarly, LY294002 and Wortmannin are potent inhibitors of phosphoinositide 3-kinases (PI3K), which are involved in numerous cellular functions. Their inhibition by these chemicals can disrupt the phosphorylation state of a range of proteins, including those that regulate the activity of ZNF323, leading to a decrease in ZNF323's functional output.

Beyond the phosphorylation-centric mechanisms, other inhibitors such as Trichostatin A and C646 disrupt the protein's function by altering the chromatin state. Trichostatin A inhibits histone deacetylases, which can change gene expression profiles and protein interactions that ZNF323 is involved in, while C646 targets the histone acetyltransferase p300. This can affect histone acetylation, thereby potentially influencing ZNF323's DNA-binding activity. RG108 and 5-Azacytidine influence DNA methylation patterns, with RG108 inhibiting DNA methyltransferases and 5-Azacytidine causing DNA demethylation; these changes in the DNA methylation landscape can impact ZNF323's ability to bind to DNA, thus inhibiting its function. Further, the MAPK pathway inhibitors PD98059, SP600125, SB203580, and U0126 also play roles in modulating ZNF323 activity. PD98059 and U0126 inhibit MEK1/2, which are part of the MAPK/ERK pathway, a pathway that has been implicated in the regulation of a variety of proteins, including ZNF323. SP600125 and SB203580 specifically inhibit JNK and p38 MAP Kinase, respectively, which could lead to reduced phosphorylation levels of proteins that interact with ZNF323, culminating in a decrease in the functional activity of ZNF323.

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