Deacetylase and Histone Modification
Items 91 to 100 of 134 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Gliotoxin | 67-99-2 | sc-201299 sc-201299A | 2 mg 10 mg | $134.00 $394.00 | 1 | |
Gliotoxin functions as a potent deacetylase inhibitor, engaging in specific interactions with histone proteins that modulate their acetylation status. Its unique binding affinity alters the conformational dynamics of histone deacetylases, impacting their enzymatic activity. This compound can induce a shift in the epigenetic landscape, influencing chromatin accessibility and stability, which may lead to profound effects on transcriptional regulation and cellular signaling pathways. | ||||||
Acetyl chloride | 75-36-5 | sc-207253 sc-207253A | 25 g 500 g | $31.00 $51.00 | ||
Acetyl chloride acts as a reactive acylating agent, facilitating the formation of acyl derivatives through its electrophilic carbonyl carbon. As a deacetylase inhibitor, it selectively modifies histone proteins, disrupting their acetylation balance. This alteration can influence the structural integrity of chromatin, affecting gene expression. Its rapid reactivity with nucleophiles allows for precise modulation of histone interactions, thereby impacting cellular processes and epigenetic regulation. | ||||||
Indole-3-acetamide | 879-37-8 | sc-255213 sc-255213A | 1 g 5 g | $44.00 $198.00 | 1 | |
Indole-3-acetamide functions as a potent deacetylase inhibitor, engaging in specific hydrogen bonding and π-π stacking interactions with histone proteins. This compound alters the acetylation state of histones, leading to significant changes in chromatin architecture. Its unique ability to stabilize histone conformations can modulate transcriptional activity, influencing cellular signaling pathways. The compound's kinetic profile allows for targeted intervention in epigenetic mechanisms, showcasing its role in chromatin dynamics. | ||||||
Daminozide | 1596-84-5 | sc-326749 sc-326749A | 5 g 25 g | $33.00 $82.00 | ||
Daminozide acts as a deacetylase inhibitor by selectively disrupting the interaction between histones and acetyl groups, thereby influencing the epigenetic landscape. Its unique structure facilitates specific van der Waals forces and hydrophobic interactions with histone tails, promoting altered gene expression patterns. The compound's reactivity and binding affinity contribute to its ability to modulate chromatin accessibility, impacting various cellular processes and regulatory networks. | ||||||
trans 2-Phenylcyclopropylamine Hydrochloride | 1986-47-6 | sc-208452 sc-208452A | 250 mg 1 g | $57.00 $166.00 | 1 | |
Trans 2-Phenylcyclopropylamine Hydrochloride functions as a deacetylase inhibitor by engaging in specific hydrogen bonding and π-π stacking interactions with histone proteins. This compound's unique cyclopropyl structure enhances its conformational flexibility, allowing it to effectively disrupt the deacetylation process. Its kinetic profile indicates a rapid association with target enzymes, leading to significant alterations in chromatin structure and gene regulation, thereby influencing cellular dynamics. | ||||||
Bufexamac | 2438-72-4 | sc-227537 | 10 g | $75.00 | ||
Bufexamac acts as a deacetylase inhibitor through its ability to form stable complexes with histone proteins, primarily via hydrophobic interactions and electrostatic forces. Its unique structural features facilitate selective binding to the active sites of deacetylases, modulating their enzymatic activity. The compound exhibits a distinct reaction kinetics profile, characterized by a delayed dissociation rate, which enhances its efficacy in altering histone acetylation patterns and influencing epigenetic regulation. | ||||||
1-Acetylimidazole | 2466-76-4 | sc-253880 | 25 g | $40.00 | ||
1-Acetylimidazole functions as a deacetylase inhibitor by engaging in specific hydrogen bonding and π-π stacking interactions with histone proteins. Its unique imidazole ring structure allows for precise recognition of deacetylase active sites, leading to effective modulation of enzymatic activity. The compound's reactivity is influenced by its electrophilic nature, promoting selective acetylation of target residues, thereby impacting chromatin dynamics and gene expression regulation. | ||||||
NSC 3852 | 3565-26-2 | sc-205773 sc-205773A | 10 mg 50 mg | $102.00 $173.00 | ||
NSC 3852 acts as a deacetylase inhibitor through its ability to form stable complexes with histone proteins, leveraging its unique structural features to disrupt enzyme-substrate interactions. The compound exhibits a distinctive binding affinity, facilitating alterations in histone acetylation patterns. Its kinetic profile reveals a competitive inhibition mechanism, which can significantly influence chromatin remodeling processes and downstream cellular signaling pathways. | ||||||
Chitosan | 9012-76-4 | sc-221421 sc-221421A sc-221421B sc-221421D sc-221421C | 10 g 25 g 100 g 8 kg 500 g | $41.00 $55.00 $135.00 $3339.00 $298.00 | 6 | |
Chitosan functions as a deacetylase inhibitor by engaging in specific interactions with histone proteins, characterized by its unique polysaccharide structure. This interaction alters the dynamics of histone modification, impacting gene expression regulation. The compound's ability to form hydrogen bonds and hydrophobic interactions enhances its binding stability, leading to significant changes in chromatin architecture. Its influence on acetylation dynamics can modulate various cellular processes, reflecting its role in epigenetic regulation. | ||||||
Sangivamycin | 18417-89-5 | sc-204261 sc-204261A sc-204261B sc-204261C sc-204261D sc-204261E | 1 mg 10 mg 25 mg 50 mg 100 mg 250 mg | $333.00 $1348.00 $2611.00 $5212.00 $9894.00 $20298.00 | ||
Sangivamycin acts as a deacetylase inhibitor through its distinctive purine-like structure, which allows it to effectively bind to histone deacetylases. This binding disrupts the enzyme's active site, influencing the acetylation status of histones and thereby altering chromatin remodeling. The compound's unique molecular interactions, including π-π stacking and electrostatic interactions, enhance its specificity and efficacy in modulating histone dynamics, ultimately affecting transcriptional regulation. | ||||||