Deacetylase and Histone Modification
Items 61 to 70 of 134 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Tenovin-1 | 380315-80-0 | sc-222342 | 10 mg | $89.00 | 1 | |
Tenovin-1 functions as a potent deacetylase inhibitor, exhibiting a unique ability to disrupt the interaction between deacetylases and their substrates. Its specific binding affinity alters the conformational dynamics of histone proteins, impacting the accessibility of chromatin. This modulation of histone acetylation status can significantly influence epigenetic regulation, affecting transcriptional activity and cellular signaling pathways through intricate molecular mechanisms. | ||||||
CI 994 | 112522-64-2 | sc-205245 sc-205245A | 10 mg 50 mg | $99.00 $536.00 | 1 | |
CI 994 acts as a selective deacetylase inhibitor, engaging in specific interactions with the active sites of histone deacetylases. By stabilizing the acetylated form of histones, it alters the structural conformation of chromatin, enhancing the recruitment of transcriptional co-activators. This compound exhibits unique kinetics, influencing the rate of deacetylation and promoting a dynamic balance in histone modifications, thereby impacting gene expression regulation at a molecular level. | ||||||
LAQ824 | 404951-53-7 | sc-364521 sc-364521A | 10 mg 50 mg | $225.00 $1000.00 | ||
LAQ824 functions as a potent deacetylase inhibitor, selectively targeting histone deacetylases to modulate chromatin dynamics. Its unique binding affinity disrupts the deacetylation process, leading to an accumulation of acetylated histones. This alteration in histone modification patterns influences chromatin accessibility and stability, facilitating distinct transcriptional outcomes. The compound's interaction with specific residues in the enzyme's active site underscores its role in fine-tuning epigenetic regulation. | ||||||
Mocetinostat | 726169-73-9 | sc-364539 sc-364539B sc-364539A | 5 mg 10 mg 50 mg | $214.00 $247.00 $1463.00 | 2 | |
Mocetinostat acts as a selective deacetylase inhibitor, engaging with histone deacetylases to alter the acetylation landscape of chromatin. Its unique mechanism involves forming stable interactions with key amino acid residues, which hinders the enzymatic activity and promotes histone acetylation. This modulation of histone marks can significantly impact gene expression profiles, enhancing chromatin fluidity and influencing cellular processes through epigenetic modifications. | ||||||
CUDC-101 | 1012054-59-9 | sc-364474 sc-364474A | 10 mg 50 mg | $190.00 $700.00 | ||
CUDC-101 functions as a potent deacetylase inhibitor, targeting histone deacetylases to disrupt the balance of acetylation in chromatin. Its distinct binding affinity allows it to interact with specific residues within the enzyme's active site, effectively blocking substrate access. This inhibition leads to an accumulation of acetylated histones, which can alter chromatin structure and dynamics, thereby influencing transcriptional regulation and cellular signaling pathways through epigenetic alterations. | ||||||
AN-9 | 122110-53-6 | sc-364403 sc-364403A | 5 mg 25 mg | $72.00 $269.00 | ||
AN-9 functions as a potent deacetylase inhibitor, engaging in specific interactions with the active site of histone deacetylases. Its unique molecular architecture allows for enhanced binding affinity, disrupting the enzyme's catalytic activity. This inhibition alters the acetylation landscape of histones, influencing chromatin structure and dynamics. The compound's kinetic profile suggests a rapid onset of action, facilitating significant alterations in cellular signaling pathways and gene regulation. | ||||||
PTACH | 848354-66-5 | sc-253326 | 2 mg | $216.00 | ||
PTACH acts as a selective deacetylase inhibitor, characterized by its ability to form stable complexes with histone deacetylases. Its unique structural features promote specific hydrogen bonding and hydrophobic interactions, enhancing its binding efficiency. This compound modulates the acetylation status of histones, leading to profound changes in chromatin accessibility and gene expression. Additionally, PTACH exhibits a distinctive reaction kinetics profile, allowing for nuanced regulation of cellular processes. | ||||||
L-Lysine | 56-87-1 | sc-207804 sc-207804A sc-207804B | 25 g 100 g 1 kg | $95.00 $263.00 $529.00 | ||
L-Lysine functions as a potent deacetylase inhibitor, engaging in specific interactions with histone proteins that alter their acetylation state. Its unique amino acid structure facilitates strong ionic and hydrogen bonding with target enzymes, influencing chromatin dynamics. This modulation of histone deacetylation impacts gene regulation pathways, while L-Lysine's kinetic properties allow for precise control over cellular signaling mechanisms, contributing to the intricate balance of gene expression. | ||||||
BML-266 | 96969-83-4 | sc-221371 sc-221371A | 10 mg 50 mg | $173.00 $666.00 | 1 | |
BML-266 acts as a selective deacetylase inhibitor, exhibiting a unique ability to disrupt the interaction between histones and deacetylase enzymes. Its structural features enable it to form stable complexes, influencing the conformational dynamics of chromatin. This compound alters the acetylation landscape, thereby modulating transcriptional activity. The reaction kinetics of BML-266 suggest a nuanced engagement with enzymatic pathways, providing insights into the regulation of epigenetic modifications. | ||||||
Droxinostat | 99873-43-5 | sc-364485 sc-364485A | 5 mg 25 mg | $85.00 $454.00 | 1 | |
Droxinostat functions as a potent deacetylase inhibitor, characterized by its ability to selectively target histone deacetylases. Its unique molecular structure facilitates specific binding interactions, leading to alterations in histone acetylation patterns. This compound influences chromatin architecture, promoting a more relaxed state conducive to transcriptional regulation. The kinetics of Droxinostat reveal a complex interplay with enzymatic mechanisms, shedding light on the dynamics of epigenetic control. | ||||||