Date published: 2025-9-12

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ZNF28 Inhibitors

Chemical inhibitors of ZNF28 include a variety of compounds that interfere with different cellular signaling pathways and mechanisms to inhibit the functional activity of the protein. Alsterpaullone targets cyclin-dependent kinases, which are essential for cell cycle progression. Inhibition of these kinases by Alsterpaullone can disrupt the cell cycle-dependent regulation of ZNF28, potentially leading to its functional inhibition. GW5074 and PD98059 act upon the MAPK/ERK pathway, with GW5074 inhibiting c-Raf kinase and PD98059 targeting MEK. These actions prevent the phosphorylation events necessary for ZNF28's activity, leading to its functional inhibition. SP600125 exerts its effect by inhibiting JNK, which is implicated in transcription factor regulation, potentially affecting ZNF28's phosphorylation state and activity.

Furthermore, LY294002, a PI3K inhibitor, disrupts the PI3K/Akt pathway, which has critical roles in regulating transcription factors, thereby affecting ZNF28's functional activity. Rapamycin inhibits mTOR, which is involved in protein synthesis and the regulation of transcription factors, leading to the functional inhibition of ZNF28 by affecting its regulation or stability. SB203580, a p38 MAP kinase inhibitor, impacts transcription factor activity, and thus, the inhibition of p38 MAP kinase can result in the functional inhibition of ZNF28. Proteasome inhibitors such as MG132 and Bortezomib prevent the degradation of proteins that participate in crucial signaling pathways, such as the NF-κB pathway, which can be necessary for the regulation or activity of ZNF28. Mitoxantrone, by inhibiting topoisomerase II, affects DNA repair and replication processes, which can lead to the functional inhibition of ZNF28. Chelerythrine, which inhibits protein kinase C, impacts signal transduction pathways that regulate transcription factors, and thus, inhibiting PKC can lead to ZNF28's functional inhibition. Lastly, 5-Azacytidine, by inhibiting DNA methyltransferases, can alter the methylation status of genes and their expression patterns, which could affect ZNF28's binding sites or regulatory regions, leading to its functional inhibition.

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