Date published: 2025-10-13

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C19orf50 Inhibitors

C19orf50 inhibitors are compounds that affect the activity of the protein C19orf50 by targeting various cellular processes that are upstream or integral to its function. The histone deacetylase inhibitors, such as Trichostatin A, Vorinostat, Entinostat, and Romidepsin, function by increasing histone acetylation, leading to a more relaxed chromatin state. This relaxed state can reduce C19orf50's ability to access and bind to its target DNA sequences within the chromatin, as C19orf50 might preferentially interact with DNA in a more compacted form. The acetylated chromatin structure may also affect the recruitment of co-factors required for C19orf50's activity, further inhibiting its function.

In addition, inhibitors like 5-Azacytidine, RG108, and Decitabine modulate the methylation status of DNA. By inhibiting DNA methyltransferase activity, these compounds decrease DNA methylation levels, which can hinder C19orf50's ability to recognize and bind to its target methylated DNA regulatory regions. This disruption of DNA-protein interactions can lead to decreased functional activity of C19orf50. Proteasome inhibitors such as MG132 may lead to increased levels of proteins that can bind to and sequester C19orf50 or its co-factors, further inhibiting its functional activity. Cell cycle modulation by PD0332991, as well as transcriptional inhibition by Triptolide, represent additional strategies that indirectly lead to a reduction in C19orf50's target gene expression. A-366, targeting histone methylation, may alter the recruitment of C19orf50 to its binding sites.

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