Histone cluster 2 H3C2 Inhibitors
Chemical inhibitors of Histone cluster 2 H3C2 operate through the inhibition of histone deacetylases (HDACs), enzymes that remove acetyl groups from the ε-N-acetyl lysine amino acids on histones. The removal of acetyl groups by HDACs leads to a closed chromatin conformation and reduced gene expression. The inhibitors, by blocking HDAC activity, cause an accumulation of acetylation on histones including Histone cluster 2 H3C2. This hyperacetylation results in a more relaxed chromatin structure, which can interfere with the normal interactions between Histone cluster 2 H3C2 and DNA, as well as between the histone and other histone proteins. Trichostatin A, Mocetinostat, Entinostat, Panobinostat, Vorinostat, Belinostat, Romidepsin, Valproic acid, Sodium butyrate, SAHA, LMK-235, and CUDC-101 are all compounds that act on this epigenetic regulation mechanism. Each of these compounds has a specific or broad spectrum of activity against different classes of HDACs, but all lead to increased acetylation of Histone cluster 2 H3C2, affecting its function and the overall chromatin landscape.
The specific action of these inhibitors varies, with some exhibiting selectivity for certain HDAC classes. For instance, Mocetinostat targets class I and IV HDACs, while Entinostat is more specific for class I HDACs, and Panobinostat is known for its broad-spectrum HDAC inhibitory activity. Regardless of their specificity, the end result is the elevation of Histone cluster 2 H3C2 acetylation. This modification can disrupt the normal function of Histone cluster 2 H3C2 in chromatin remodeling and gene expression regulation. Vorinostat and SAHA, which are structurally similar, both lead to the accumulation of acetylated Histone cluster 2 H3C2, potentially changing the interaction of the histone with chromatin. LMK-235 and CUDC-101, although not as widely studied, also contribute to this increase in acetylation, thereby altering the function of Histone cluster 2 H3C2 and its role in the regulation of gene expression.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Trichostatin A | 58880-19-6 | sc-3511 sc-3511A sc-3511B sc-3511C sc-3511D | 1 mg 5 mg 10 mg 25 mg 50 mg | $152.00 $479.00 $632.00 $1223.00 $2132.00 | 33 | |
Inhibits histone deacetylases (HDACs), leading to increased acetylation of histones like Histone cluster 2 H3C2, which can result in the chromatin becoming too open, thus interfering with the normal transcription process that relies on properly acetylated Histone cluster 2 H3C2. | ||||||
Mocetinostat | 726169-73-9 | sc-364539 sc-364539B sc-364539A | 5 mg 10 mg 50 mg | $214.00 $247.00 $1463.00 | 2 | |
Inhibits class I and IV HDACs, thereby increasing histone acetylation, which affects the Histone cluster 2 H3C2 by altering its interaction with DNA and other histones, potentially disrupting the chromatin structure and function. | ||||||
MS-275 | 209783-80-2 | sc-279455 sc-279455A sc-279455B | 1 mg 5 mg 25 mg | $24.00 $90.00 $212.00 | 24 | |
Specifically inhibits class I HDACs, leading to hyperacetylation of Histone cluster 2 H3C2, which can prevent the normal functioning of the histone, thereby inhibiting its role in chromatin remodeling and gene expression. | ||||||
Panobinostat | 404950-80-7 | sc-208148 | 10 mg | $200.00 | 9 | |
A potent pan-HDAC inhibitor that increases acetylation of histones including Histone cluster 2 H3C2, which can disrupt normal chromatin dynamics and transcriptional activities where Histone cluster 2 H3C2 is involved. | ||||||
Suberoylanilide Hydroxamic Acid | 149647-78-9 | sc-220139 sc-220139A | 100 mg 500 mg | $133.00 $275.00 | 37 | |
Inhibits HDAC activity, leading to the accumulation of acetylated histones such as Histone cluster 2 H3C2, which can alter chromatin structure and hinder the protein's normal function in the regulation of gene expression. | ||||||
Belinostat | 414864-00-9 | sc-269851 sc-269851A | 10 mg 100 mg | $156.00 $572.00 | ||
HDAC inhibitor that increases acetylation levels of histone proteins including Histone cluster 2 H3C2, potentially disrupting the chromatin compaction and gene expression processes that involve this histone. | ||||||
Romidepsin | 128517-07-7 | sc-364603 sc-364603A | 1 mg 5 mg | $218.00 $634.00 | 1 | |
Targets HDACs, causing an increase in acetylated Histone cluster 2 H3C2, which may interfere with its normal role in chromatin architecture and transcriptional regulation. | ||||||
Valproic Acid | 99-66-1 | sc-213144 | 10 g | $87.00 | 9 | |
HDAC inhibitor that can lead to hyperacetylation of Histone cluster 2 H3C2, affecting chromatin structure and function, thus inhibiting the histone's normal role in gene expression. | ||||||
Sodium Butyrate | 156-54-7 | sc-202341 sc-202341B sc-202341A sc-202341C | 250 mg 5 g 25 g 500 g | $31.00 $47.00 $84.00 $222.00 | 19 | |
Inhibits HDACs, causing increased acetylation of histones including Histone cluster 2 H3C2, which can alter its function in chromatin remodeling and gene regulation. | ||||||