Histone cluster 1 H1C Inhibitors
Histone cluster 1 H1C inhibitors are a class of chemical compounds specifically designed to target and interact with a particular group of proteins known as histone cluster 1 H1C. These inhibitors are primarily employed in molecular and cellular biology research to modulate the activity of histone cluster 1 H1C proteins within the context of chromatin structure and gene regulation. Histone cluster 1 H1C proteins are a subset of histones, which are essential components of chromatin-a complex of DNA and proteins found within the nucleus of eukaryotic cells. These proteins play a pivotal role in regulating gene expression by packaging DNA into a condensed and organized structure, thereby influencing the accessibility of genetic information to the cellular machinery.
Histone cluster 1 H1C inhibitors work by selectively binding to histone cluster 1 H1C proteins, altering their conformation or function. This interaction can lead to changes in chromatin structure and, consequently, affect gene expression patterns. Researchers utilize these inhibitors to investigate the intricacies of chromatin dynamics, epigenetic modifications, and gene regulation in various cellular processes. Understanding the mechanisms behind histone cluster 1 H1C inhibition can shed light on fundamental biological processes, including development, differentiation, and disease progression. By probing the role of histone cluster 1 H1C proteins in chromatin remodeling, scientists aim to unravel the complexities of gene regulation and potentially identify new avenues for future research.
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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 | $149.00 $470.00 $620.00 $1199.00 $2090.00 | 33 | |
Inhibits histone deacetylases, leading to increased acetylation of histones, which can reduce the binding affinity of H1-2 to DNA, thus influencing chromatin structure. | ||||||
Suberoylanilide Hydroxamic Acid | 149647-78-9 | sc-220139 sc-220139A | 100 mg 500 mg | $130.00 $270.00 | 37 | |
A histone deacetylase inhibitor that increases acetylation levels of histones, thereby potentially decreasing the interaction of H1-2 with chromatin. | ||||||
Sodium Butyrate | 156-54-7 | sc-202341 sc-202341B sc-202341A sc-202341C | 250 mg 5 g 25 g 500 g | $30.00 $46.00 $82.00 $218.00 | 19 | |
Histone deacetylase inhibitor that causes hyperacetylation of histones, which can affect H1-2's role in chromatin condensation and gene regulation. | ||||||
Mocetinostat | 726169-73-9 | sc-364539 sc-364539B sc-364539A | 5 mg 10 mg 50 mg | $210.00 $242.00 $1434.00 | 2 | |
A selective inhibitor of histone deacetylases, altering acetylation status of histones and potentially impacting H1-2 function. | ||||||
Belinostat | 414864-00-9 | sc-269851 sc-269851A | 10 mg 100 mg | $153.00 $561.00 | ||
Histone deacetylase inhibitor that can modify histone acetylation and potentially affect H1-2's chromatin association. | ||||||
Panobinostat | 404950-80-7 | sc-208148 | 10 mg | $196.00 | 9 | |
A potent histone deacetylase inhibitor that can lead to changes in chromatin structure and potentially influence H1-2 interaction with DNA. | ||||||
Romidepsin | 128517-07-7 | sc-364603 sc-364603A | 1 mg 5 mg | $214.00 $622.00 | 1 | |
Acts on histone deacetylases to alter the acetylation state of histones, which can impact H1-2's chromatin-related functions. | ||||||
Valproic Acid | 99-66-1 | sc-213144 | 10 g | $85.00 | 9 | |
A histone deacetylase inhibitor that can lead to hyperacetylation of histones and affect H1-2's role in chromatin structure and function. | ||||||
MS-275 | 209783-80-2 | sc-279455 sc-279455A sc-279455B | 1 mg 5 mg 25 mg | $24.00 $88.00 $208.00 | 24 | |
Selectively inhibits histone deacetylases, potentially affecting the interaction of H1-2 with chromatin. | ||||||
ITF2357 | 732302-99-7 | sc-364513 sc-364513A | 5 mg 50 mg | $340.00 $1950.00 | ||
Inhibitor of histone deacetylases that can cause changes in chromatin architecture, potentially affecting H1-2's function. | ||||||