The inhibition of the protein histone H2A, a key component in the structure and function of chromatin, can be achieved through the alteration of its interaction with DNA, primarily via the process of acetylation. Chemicals like Trichostatin A, Vorinostat, Panobinostat, Entinostat, Romidepsin, Belinostat, Quisinostat, Givinostat, CUDC-101, Mocetinostat, Tacedinaline, and Valproic Acid, all function as inhibitors of histone deacetylases (HDACs). These inhibitors lead to an increase in the acetylation levels of histone H2A. Hyperacetylation of histone H2A disrupts its ability to tightly package DNA within the chromatin structure, thereby inhibiting its essential role in chromatin remodeling and gene regulation. The increased acetylation caused by these chemicals alters the interaction between histone H2A and DNA, weakening the histone-DNA binding that is necessary for maintaining the condensed structure of chromatin. This relaxation of chromatin structure can have significant implications on the accessibility of DNA for transcription and, consequently, on gene expression patterns.
The specific action of these HDAC inhibitors on histone H2A elucidates the intricate balance of histone modifications in regulating chromatin dynamics and gene expression. The inhibitors like Vorinostat and Romidepsin, by increasing the acetylation of histone H2A, impair its ability to effectively condense DNA, which is crucial for the proper regulation of gene expression and maintenance of chromatin structure. Additionally, chemicals such as Entinostat and Belinostat, through selective inhibition of class I HDACs, further underscore the specificity of histone modification in controlling chromatin architecture. This hyperacetylation leads to a more open chromatin state, reducing the efficiency of histone H2A in packaging DNA and thereby inhibiting its traditional role in chromatin organization. These inhibitors collectively demonstrate the pivotal role of histone acetylation in the functional regulation of histone H2A and provide insight into the mechanisms by which chromatin structure and function can be modulated at the molecular level.d
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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 inhibits histone deacetylases, leading to hyperacetylation which can disrupt the interaction between histone H2A and DNA, thus inhibiting the protein's role in chromatin remodeling. | ||||||
Suberoylanilide Hydroxamic Acid | 149647-78-9 | sc-220139 sc-220139A | 100 mg 500 mg | $133.00 $275.00 | 37 | |
Suberoylanilide Hydroxamic Acid, a histone deacetylase inhibitor, causes increased acetylation of histone H2A, impairing its ability to condense DNA effectively, thereby inhibiting its function in maintaining chromatin structure. | ||||||
Panobinostat | 404950-80-7 | sc-208148 | 10 mg | $200.00 | 9 | |
Panobinostat, another histone deacetylase inhibitor, leads to the hyperacetylation of histone H2A, disrupting its interaction with DNA and other histones, which inhibits its structural role in chromatin. | ||||||
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 class I histone deacetylases, causing hyperacetylation of histone H2A, which affects its ability to package DNA tightly, thus inhibiting its normal function. | ||||||
Romidepsin | 128517-07-7 | sc-364603 sc-364603A | 1 mg 5 mg | $218.00 $634.00 | 1 | |
Romidepsin inhibits histone deacetylase, leading to increased acetylation of histone H2A, which disrupts its ability to maintain chromatin structure, thereby inhibiting its functional role. | ||||||
Belinostat | 414864-00-9 | sc-269851 sc-269851A | 10 mg 100 mg | $156.00 $572.00 | ||
Belinostat is a histone deacetylase inhibitor that increases the acetylation of histone H2A, affecting its interaction with DNA and inhibiting its role in chromatin remodeling and gene regulation. | ||||||
JNJ-26481585 | 875320-29-9 | sc-364515 sc-364515A | 5 mg 50 mg | $321.00 $1224.00 | ||
JNJ-26481585 inhibits histone deacetylase, leading to the hyperacetylation of histone H2A, which disrupts its normal function in chromatin structure and gene expression regulation. | ||||||
ITF2357 | 732302-99-7 | sc-364513 sc-364513A | 5 mg 50 mg | $340.00 $1950.00 | ||
ITF2357 inhibits histone deacetylase, increasing acetylation levels of histone H2A and thereby inhibiting its role in maintaining the structural integrity of chromatin. | ||||||
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 causes hyperacetylation of histone H2A, disrupting its ability to compact DNA and thus inhibiting its functional role in chromatin structure. | ||||||
CI 994 | 112522-64-2 | sc-205245 sc-205245A | 10 mg 50 mg | $99.00 $536.00 | 1 | |
CI 994 inhibits histone deacetylase, leading to the hyperacetylation of histone H2A, thereby affecting its role in DNA packaging and chromatin organization, and inhibiting its function. | ||||||