Date published: 2025-10-31

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C6orf225 Inhibitors

Chemical inhibitors of C6orf225 encompass a variety of compounds that target specific signaling pathways and kinases involved in the regulation and activity of this protein. Staurosporine, a potent kinase inhibitor, can disrupt the phosphorylation processes vital to C6orf225's function by binding to the ATP-binding sites of kinases within its signaling pathways. Similarly, the PI3K inhibitors Wortmannin and LY294002 can impede the PI3K/AKT/mTOR signaling pathway, leading to a reduction in the activation and subsequent phosphorylation of proteins such as C6orf225. Rapamycin specifically inhibits mTOR, a central component of the pathway responsible for protein synthesis and function, thus also affecting the activity of C6orf225.

Other inhibitors target different aspects of cellular signaling that can influence C6orf225. PD98059 and U0126, both MEK inhibitors, can prevent the activation of the ERK/MAPK signaling pathway, which is fundamental to numerous cellular activities. By inhibiting MEK, these compounds can reduce the activity of proteins that operate within this cascade, including C6orf225. The JNK signaling pathway, which can be suppressed by the JNK inhibitor SP600125, and the p38 MAPK signaling pathway, targeted by SB203580, are critical for stress responses and cytokine production. Inhibition of these pathways can result in the decreased function of relevant proteins like C6orf225. Moreover, Dasatinib and PP2 inhibit Src family kinases and Abl, which could decrease the function of proteins regulated by these kinases, including C6orf225. Finally, inhibitors such as Bisindolylmaleimide I and Go6983 target protein kinase C (PKC), leading to a reduction in PKC-mediated signaling pathways. As PKC is essential for the phosphorylation and activity of many proteins, the inhibition by these compounds can lead to decreased functionality of proteins like C6orf225 that may be regulated by PKC-dependent phosphorylation.

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