Deacetylase and Histone Modification
Items 131 to 134 of 134 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Fmoc-L-Lys(Me2)-OH*HCl | 252049-10-8 | sc-294919 | 250 mg | $300.00 | ||
Fmoc-L-Lys(Me2)-OH*HCl acts as a potent deacetylase inhibitor, characterized by its unique side chain modifications that enhance binding affinity to histone deacetylases. The presence of the Fmoc group allows for specific π-π stacking interactions, while the dimethylated lysine residue introduces steric hindrance, altering enzyme kinetics. This compound's ability to stabilize enzyme-substrate complexes can significantly influence histone acetylation dynamics, thereby affecting chromatin structure and gene expression. | ||||||
HNHA | 926908-04-5 | sc-205343 sc-205343A | 5 mg 10 mg | $161.00 $405.00 | ||
HNHA functions as a selective deacetylase inhibitor, distinguished by its unique structural features that facilitate strong interactions with histone deacetylases. Its specific functional groups promote hydrogen bonding and hydrophobic interactions, enhancing binding specificity. The compound's kinetic profile reveals a competitive inhibition mechanism, which modulates the activity of deacetylases, ultimately impacting histone modification patterns and chromatin remodeling processes. | ||||||
SB939 | 929016-96-6 | sc-364610 sc-364610A | 5 mg 50 mg | $209.00 $851.00 | ||
SB939 is a potent deacetylase inhibitor characterized by its ability to disrupt the interaction between histones and deacetylases through unique molecular conformations. Its distinct binding affinity is attributed to specific electrostatic interactions and steric hindrance, which alter the enzyme's active site dynamics. This compound exhibits a non-linear reaction kinetics profile, influencing the rate of histone acetylation and subsequent chromatin accessibility, thereby affecting gene expression regulation. | ||||||
Coumarin-SAHA | 1260635-77-5 | sc-391815 sc-391815A | 1 mg 10 mg | $56.00 $216.00 | ||
Coumarin-SAHA functions as a deacetylase inhibitor by engaging in selective binding with histone deacetylases, leading to conformational changes that hinder their enzymatic activity. Its unique structural features facilitate strong hydrogen bonding and hydrophobic interactions, enhancing its specificity. The compound's kinetic behavior reveals a complex modulation of histone acetylation rates, impacting chromatin structure and influencing transcriptional regulation through altered protein interactions. | ||||||