Date published: 2025-9-11

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ZNF493 Inhibitors

Chemical inhibitors of ZNF493 can exert their inhibitory effects through various mechanisms by targeting specific kinases and signaling pathways that are essential for the functional activity of the protein. Staurosporine, a broad-spectrum kinase inhibitor, can inhibit the protein kinases responsible for the phosphorylation of ZNF493, which is a critical post-translational modification required for its activation. Similarly, LY294002, a PI3K inhibitor, disrupts the PI3K/AKT signaling pathway, impairing the phosphorylation and consequently the functional activity of ZNF493. The MEK inhibitor PD98059 can hinder the ERK/MAPK pathway, reducing the phosphorylation of proteins in this signaling cascade, which includes ZNF493, thereby inhibiting its functional response. Rapamycin, by inhibiting mTOR, influences the PI3K/AKT/mTOR pathway, which plays a role in regulating protein synthesis and could lead to the functional inhibition of ZNF493.

Furthermore, SB203580's inhibition of p38 MAP Kinase can prevent the signaling that may activate ZNF493, while U0126's inhibition of MEK1/2 similarly suppresses the ERK/MAPK pathway's influence on ZNF493's activity. The PI3K inhibitor Wortmannin also interrupts signaling pathways critical for ZNF493's phosphorylation, while SP600125, a JNK inhibitor, can block signaling pathways that are implicated in the regulation of ZNF493's functional activity. Moreover, Y-27632 inhibition of ROCK potentially alters downstream signaling necessary for ZNF493's role in cellular processes. Gefitinib's targeting of EGFR disrupts upstream signals that converge on pathways regulating ZNF493. Further disruption of cell cycle-related processes by VX-680's inhibition of Aurora kinases and Palbociclib's inhibition of CDK4/6 could also lead to the suppression of ZNF493's function within these cellular contexts, as these processes can be important for the proper activity and regulation of ZNF493.

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