OTTMUSG00000018481 Inhibitors
The inhibition of histone H2A, a core component of the nucleosome involved in the structural organization of chromatin and regulation of gene expression, can be achieved through various chemical inhibitors that primarily target histone deacetylases (HDACs). These inhibitors, such as Trichostatin A, Vorinostat, Panobinostat, Belinostat, Romidepsin, Sodium butyrate, Valproic acid, Entinostat, Mocetinostat, SAHA, Givinostat, and Scriptaid, function by preventing the deacetylation of histone H2A. This prevention leads to an increase in the acetylation levels of histone H2A, a modification that significantly alters its interaction with DNA and other nuclear proteins. The hyperacetylation of histone H2A disrupts the chromatin structure, affecting its compaction and consequently influencing gene expression patterns. These changes are critical as they impede the functional role of histone H2A in chromatin remodeling and gene regulation, which are essential processes for normal cellular function and genomic stability.
The specific action of these inhibitors on histone deacetylases results in an altered chromatin landscape, where the increased acetylation of histone H2A impacts its ability to maintain the typical chromatin structure. This structural alteration leads to changes in the accessibility of DNA to various transcription factors and other chromatin-associated proteins, thereby modulating gene expression. The inhibitors, by increasing the acetylation levels of histone H2A, interfere with the normal histone-DNA interactions and the interaction of histones with other proteins involved in the formation of the nucleosome structure. This interference ultimately results in the inhibition of the normal activities of histone H2A, which include its role in the structural organization of chromatin, the regulation of gene expression, and the maintenance of genomic integrity. Therefore, these chemical inhibitors, through their targeted action on histone deacetylases, provide a means to modulate the function of histone H2A, showcasing the intricate interplay between histone modifications and chromatin dynamics.
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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 | |
Trichostatin A is a histone deacetylase inhibitor. It inhibits the deacetylation of histones, including histone H2A, which leads to an increase in the acetylation levels of these proteins. This hyperacetylation of histone H2A alters its interaction with DNA and other nuclear proteins, inhibiting its normal function in chromatin remodeling and gene regulation. | ||||||
Suberoylanilide Hydroxamic Acid | 149647-78-9 | sc-220139 sc-220139A | 100 mg 500 mg | $133.00 $275.00 | 37 | |
Suberoylanilide Hydroxamic Acid, another histone deacetylase inhibitor, functions similarly to Trichostatin A. It increases the acetylation levels of histone H2A, disrupting its role in the structure and function of chromatin. The increased acetylation alters the histone’s interaction with DNA, thereby inhibiting its functional role in transcription regulation. | ||||||
Panobinostat | 404950-80-7 | sc-208148 | 10 mg | $200.00 | 9 | |
Panobinostat is a broad-spectrum histone deacetylase inhibitor. Its inhibition of histone deacetylases leads to increased acetylation of histone H2A. This modification impairs the ability of histone H2A to maintain chromatin structure, thereby inhibiting its role in gene expression control. | ||||||
Belinostat | 414864-00-9 | sc-269851 sc-269851A | 10 mg 100 mg | $156.00 $572.00 | ||
Belinostat specifically inhibits histone deacetylases. This inhibition results in increased acetylation of histone H2A, which affects its interaction with DNA and other histones, leading to an alteration in chromatin structure and function, and thus inhibiting the normal function of histone H2A. | ||||||
Romidepsin | 128517-07-7 | sc-364603 sc-364603A | 1 mg 5 mg | $218.00 $634.00 | 1 | |
Romidepsin is a histone deacetylase inhibitor that increases the acetylation levels of histone H2A. This hyperacetylation alters the structure of chromatin, affecting the function of histone H2A in gene regulation and chromatin remodeling. | ||||||
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 | |
Sodium butyrate acts as a histone deacetylase inhibitor. It leads to the accumulation of acetylated histone H2A, disrupting its normal function in chromatin structure and gene regulation by altering its interaction with DNA and other chromatin-associated proteins. | ||||||
Valproic Acid | 99-66-1 | sc-213144 | 10 g | $87.00 | 9 | |
Valproic acid, a histone deacetylase inhibitor, increases the acetylation of histone H2A. This change in acetylation status alters the interaction of histone H2A with DNA and other proteins, impacting chromatin structure and function and thus inhibiting the normal activity of histone H2A. | ||||||
MS-275 | 209783-80-2 | sc-279455 sc-279455A sc-279455B | 1 mg 5 mg 25 mg | $24.00 $90.00 $212.00 | 24 | |
MS-275 selectively inhibits histone deacetylases, leading to increased acetylation of histone H2A. This alteration in acetylation disrupts the structural and functional roles of histone H2A in chromatin, thereby inhibiting its normal regulatory functions. | ||||||
Mocetinostat | 726169-73-9 | sc-364539 sc-364539B sc-364539A | 5 mg 10 mg 50 mg | $214.00 $247.00 $1463.00 | 2 | |
Mocetinostat is a histone deacetylase inhibitor that leads to the hyperacetylation of histone H2A. This hyperacetylation changes the structure and function of chromatin, affecting the role of histone H2A in gene expression and chromatin remodeling. | ||||||
ITF2357 | 732302-99-7 | sc-364513 sc-364513A | 5 mg 50 mg | $340.00 $1950.00 | ||
ITF2357 is a histone deacetylase inhibitor. It increases the acetylation levels of histone H2A, modifying its interaction with DNA and other proteins, which in turn affects chromatin structure and function, leading to the inhibition of the normal activities of histone H2A. | ||||||