ARID2 inhibitors constitute a diverse group of chemicals designed to modulate ARID2's chromatin remodeling function, providing insights into mechanisms for cellular regulation. JQ1, a BET bromodomain inhibitor, indirectly affects ARID2 by modulating chromatin acetylation, influencing the accessibility of ARID2 to its target sites. PFI-3, targeting the PWWP domain in ARID2, disrupts its interaction with chromatin, inhibiting ARID2's function in chromatin remodeling. Additionally, inhibitors such as C646, EED226, and UNC1215 impact ARID2 indirectly by targeting histone acetyltransferases (p300) and histone methyltransferases (EZH2, G9a/GLP), altering the acetylation and methylation status of chromatin. SAHA (Vorinostat), an HDAC inhibitor, modulates ARID2 by influencing the acetylation status of histones, impacting chromatin remodeling. BAY 1238097, a SMARCA2/4 ATPase inhibitor, affects ARID2 indirectly by inhibiting the ATPase activity of SMARCA2/4 within the SWI/SNF complex.
Furthermore, CCG-1423, OTX015 (MK-8628), and EPZ005687 impact ARID2 through the inhibition of the Rho/MRTF/SRF pathway, BET bromodomains, and EZH2, respectively, altering chromatin accessibility and modulating ARID2-mediated chromatin remodeling. GSK2801 and XMD8-92 target bromodomains within BRPF1/2/3 and BRD9, respectively, disrupting interactions with chromatin and influencing ARID2 accessibility. Collectively, these inhibitors highlight the intricate interplay between chromatin dynamics and ARID2, providing valuable tools for understanding the regulation of ARID2's function in cellular processes.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
(±)-JQ1 | 1268524-69-1 | sc-472932 sc-472932A | 5 mg 25 mg | $231.00 $863.00 | 1 | |
BET bromodomain inhibitor affecting ARID2 indirectly. JQ1 modulates the acetylation status of chromatin, influencing the accessibility of ARID2 to its target sites. | ||||||
PFI 3 | 1819363-80-8 | sc-507340 | 10 mg | $300.00 | ||
Inhibitor of the PWWP domain in ARID2, preventing its interaction with chromatin. PFI-3 disrupts the binding ability of ARID2, inhibiting its function in chromatin remodeling. | ||||||
C646 | 328968-36-1 | sc-364452 sc-364452A | 10 mg 50 mg | $265.00 $944.00 | 5 | |
Inhibitor of the histone acetyltransferase p300, impacting ARID2 indirectly. C646 disrupts the acetylation processes regulated by p300, influencing the chromatin remodeling function of ARID2. | ||||||
UNC 1215 | 1415800-43-9 | sc-475020 | 10 mg | $380.00 | ||
G9a/GLP inhibitor indirectly modulating ARID2. UNC1215 targets the G9a/GLP complex, altering the methylation landscape of chromatin and impacting ARID2 function in chromatin remodeling. | ||||||
Suberoylanilide Hydroxamic Acid | 149647-78-9 | sc-220139 sc-220139A | 100 mg 500 mg | $133.00 $275.00 | 37 | |
HDAC inhibitor influencing ARID2 indirectly. SAHA modulates the acetylation status of histones, affecting the chromatin environment and influencing ARID2-mediated chromatin remodeling. | ||||||
CCG-1423 | 285986-88-1 | sc-205241 sc-205241A | 1 mg 5 mg | $30.00 $90.00 | 8 | |
Rho/MRTF/SRF pathway inhibitor indirectly affecting ARID2. CCG-1423 inhibits the Rho/MRTF/SRF pathway, disrupting the downstream signaling that modulates ARID2's chromatin remodeling activity. | ||||||
(S)-2-(4-(4-Chlorophenyl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl)-N-(4-hydroxyphenyl)acetamide | 202590-98-5 | sc-501130 | 2.5 mg | $330.00 | ||
Also called OTX015, this BET bromodomain inhibitor inhibits ARID2 indirectly. OTX015 targets the bromodomains of BET proteins, altering chromatin accessibility and impacting ARID2-mediated chromatin remodeling. | ||||||
XMD 8-92 (free base) | 1234480-50-2 | sc-364068 sc-364068A sc-364068B sc-364068C | 5 mg 10 mg 100 mg 1 g | $235.00 $340.00 $1700.00 $10330.00 | 10 | |
BRD9 bromodomain inhibitor indirectly impacting ARID2. XMD8-92 targets the bromodomain of BRD9, a subunit of the SWI/SNF complex, modulating chromatin accessibility and affecting ARID2-mediated chromatin remodeling. | ||||||