Date published: 2025-9-21

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C12orf39 Inhibitors

Chemical inhibitors of C12orf39 can exert their inhibitory effects through various biochemical pathways. Wortmannin, a known potent phosphatidylinositol 3-kinase (PI3K) inhibitor, can disrupt the PI3K-mediated signaling that is necessary for C12orf39-regulated functions, such as cellular growth or survival responses. Similarly, LY294002, another PI3K inhibitor, can dismantle the PI3K/AKT pathway, which is crucial for regulating C12orf39's activity within the cell. The interruption of this pathway can lead to a decrease in C12orf39 activity due to the lack of necessary signals for its proper function. AKT Inhibitor VIII and Triciribine, which specifically target AKT, can prevent the phosphorylation and subsequent activation of downstream targets, thereby reducing the influence of C12orf39 in metabolic processes.

Proteasome inhibitors like Bortezomib, Epoxomicin, and MG132 can prevent the degradation of proteins that regulate C12orf39's stability and function, thus indirectly maintaining a higher level of regulatory control over C12orf39. By doing so, these inhibitors can potentially lead to an accumulation of regulatory proteins that inhibit C12orf39 activity. MLN4924, on the other hand, impairs the NEDDylation pathway, which is involved in the ubiquitin-proteasome system, a cellular mechanism that could affect C12orf39's role in protein turnover. Rapamycin, an mTOR inhibitor, can disrupt the mTOR signaling pathway, which is involved in cell growth and proliferation processes that C12orf39 might be a part of. Interrupting this signaling pathway can lead to reduced C12orf39 activity. Additionally, kinase inhibitors like SB203580 and SP600125, which inhibit p38 MAP kinase and JNK respectively, can attenuate the MAPK-regulated proteins' activities, including potentially C12orf39. Palbociclib, a CDK4/6 inhibitor, can hinder the cell cycle progression, which may be essential for the function of C12orf39, leading to its functional inhibition.

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