Deacetylase and Histone Modification
Items 81 to 90 of 136 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
HC Toxin | 83209-65-8 | sc-200884 | 1 mg | $155.00 | 1 | |
HC Toxin functions as a potent deacetylase inhibitor, characterized by its ability to selectively modify histone proteins. Its unique structure facilitates strong interactions with the catalytic sites of deacetylases, leading to the stabilization of acetylated histones. This inhibition alters the epigenetic landscape, impacting chromatin structure and transcriptional regulation. The compound's reactivity as an acid halide allows for precise targeting of specific amino acid residues, enhancing its role in modulating cellular processes. | ||||||
1-Alaninechlamydocin | 141446-96-0 | sc-391717 | 500 µg | $204.00 | ||
1-Alaninechlamydocin acts as a selective deacetylase inhibitor, engaging in specific molecular interactions that disrupt the activity of histone deacetylases. Its unique conformation enables it to bind effectively to the active sites of these enzymes, promoting the accumulation of acetylated histones. This alteration in histone modification patterns influences chromatin dynamics and gene expression, while its behavior as an acid halide allows for targeted modifications at critical amino acid sites, enhancing its regulatory potential in cellular mechanisms. | ||||||
SIRT1/2 Inhibitor VII | 143034-06-4 | sc-364618 | 10 mg | $113.00 | ||
SIRT1/2 Inhibitor VII functions as a selective deacetylase inhibitor, exhibiting a unique binding affinity for the active sites of SIRT1 and SIRT2 enzymes. Its structural characteristics facilitate specific interactions that stabilize the enzyme-inhibitor complex, leading to altered histone acetylation states. This modulation of histone dynamics can significantly impact chromatin structure and transcriptional regulation, highlighting its role in cellular signaling pathways and epigenetic modifications. | ||||||
Binucleine 2 | 220088-42-6 | sc-202500 | 5 mg | $162.00 | ||
Binucleine 2 acts as a potent deacetylase inhibitor, engaging in distinctive molecular interactions that disrupt the catalytic activity of histone deacetylases. Its dual binding sites enhance specificity, promoting a conformational change in the enzyme that affects substrate accessibility. This alteration in enzyme kinetics leads to a pronounced accumulation of acetylated histones, thereby influencing chromatin remodeling and gene expression patterns, which are critical for various cellular processes. | ||||||
AK-7 | 420831-40-9 | sc-364096 sc-364096A sc-364096B | 5 mg 25 mg 100 mg | $54.00 $221.00 $880.00 | ||
AK-7 functions as a selective deacetylase inhibitor, characterized by its unique ability to stabilize the enzyme's active site through specific hydrogen bonding and hydrophobic interactions. This stabilization alters the enzyme's conformational dynamics, resulting in a significant shift in reaction kinetics. By modulating the acetylation state of histones, AK-7 plays a crucial role in regulating chromatin structure and influencing epigenetic modifications, thereby impacting cellular signaling pathways. | ||||||
(S)-HDAC-42 | 935881-37-1 | sc-296364 sc-296364A | 1 mg 5 mg | $94.00 $409.00 | ||
(S)-HDAC-42 acts as a potent deacetylase inhibitor, distinguished by its capacity to engage in specific electrostatic interactions with the enzyme's active site. This binding induces conformational changes that enhance substrate affinity and modulate catalytic efficiency. By selectively altering histone acetylation, (S)-HDAC-42 influences chromatin accessibility and stability, thereby affecting gene expression patterns and cellular processes through intricate regulatory networks. | ||||||
Pimelic Diphenylamide 106 | 937039-45-7 | sc-364589 sc-364589A | 1 mg 5 mg | $41.00 $74.00 | ||
Pimelic Diphenylamide 106 functions as a deacetylase inhibitor, characterized by its unique ability to form hydrogen bonds with key residues in the enzyme's active site. This interaction stabilizes the enzyme-substrate complex, leading to altered reaction kinetics and enhanced inhibition. By modulating histone acetylation dynamics, it plays a critical role in chromatin remodeling, influencing the structural integrity of nucleosomes and impacting transcriptional regulation through complex molecular pathways. | ||||||
TC-H 106 | 937039-45-7 | sc-362801 sc-362801A | 10 mg 50 mg | $155.00 $620.00 | ||
TC-H 106 acts as a deacetylase inhibitor, exhibiting a distinctive capacity to interact with metal ions within the enzyme's active site, which can significantly influence its catalytic efficiency. This compound alters the conformational dynamics of histones, promoting a unique balance in acetylation states. Its specific binding affinity facilitates the modulation of chromatin architecture, thereby affecting gene expression patterns through intricate regulatory networks. | ||||||
4-iodo-SAHA | 1219807-87-0 | sc-364391 sc-364391A | 50 mg 250 mg | $147.00 $663.00 | ||
4-Iodo-SAHA functions as a potent deacetylase inhibitor, characterized by its ability to form stable interactions with the enzyme's active site. This compound's unique halogen substitution enhances its binding affinity, leading to altered enzyme kinetics and modulation of histone acetylation. By influencing the structural integrity of chromatin, it plays a critical role in the dynamic regulation of epigenetic modifications, thereby impacting cellular processes at a molecular level. | ||||||
KD 5170 | 940943-37-3 | sc-362755 | 10 mg | $398.00 | ||
KD 5170 acts as a selective deacetylase inhibitor, exhibiting a unique mechanism of action through its specific interactions with histone proteins. Its structural features facilitate the disruption of hydrogen bonding within the enzyme's active site, leading to significant alterations in histone modification patterns. This compound's influence on the acetylation status of histones can result in profound changes in chromatin architecture, thereby affecting gene expression and cellular signaling pathways. | ||||||