HDAC1 Mouse Monoclonal Antibody
- Known as:
- HDAC1 Mouse Monoclonal Antibody
- Catalog number:
- BIN-003065-M11
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- HDAC1 Mouse Monoclonal Antibody
Related genes to: HDAC1 Mouse Monoclonal Antibody
- Gene:
- HDAC1 NIH gene
- Name:
- histone deacetylase 1
- Previous symbol:
- RPD3L1
- Synonyms:
- HD1, GON-10, KDAC1
- Chromosome:
- 1p35.2-p35.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-15
- Date modifiied:
- 2019-02-19
Related products to: HDAC1 Mouse Monoclonal Antibody
Related articles to: HDAC1 Mouse Monoclonal Antibody
- Histone modifications by histone deacetylases (HDACs) are essential for controlling chromatin structure and regulating gene expression. Functionally, HDACs act as enzymatic subunits within diverse multisubunit corepressor complexes, thereby targeting distinct sets of genes. Here, we identify C16orf87 as a previously uncharacterized functional subunit of the MIER corepressor complex that mediates HDAC1 and MIER1 protein interactions. Homozygous knockout of C16orf87 alters chromatin accessibility and reduces cell migration in human cells, and impairs embryonic development of zebrafish. Based on these findings, we propose renaming C16orf87 as HDAC Interacting Protein (HDIP) to reflect its newly revealed function. - Source: PubMed
Publication date: 2026/04/30
Punga TanelLarsson MårtenMujica EndrinaRabelo Melo FabioMetzendorf ChristophZhang HanqingWang Dandanden Hoed MarcelAndersson LeifParrine Débora - Valproic acid (VPA), a widely used antiepileptic drug, often induces hepatic steatosis during long-term treatment, though the underlying mechanisms remain incompletely understood. In our study, epileptic patients with abnormal liver function exhibited significantly elevated levels of homocysteine (Hcy) and glutamate (Glu) compared to those with normal liver function. Moreover, Hcy and Glu levels were positively correlated with markers of lipid accumulation and oxidative stress. Similar elevations in Hcy and Glu were observed in VPA-treated mice and hepatocyte models (HepG2, AML12), suggesting that disrupted Hcy/Glu homeostasis may be a hallmark of VPA-induced hepatic steatosis. Further in vitro experiments demonstrated that treatment with either Hcy or Glu not only increased lipid accumulation but also triggered ferroptosis, as indicated by Fe overload, suppression of the GSH-GPX4 axis, and ACSL4-mediated lipid peroxidation. These effects were attenuated by the ferroptosis inhibitor ferrostatin-1 (Fer-1), confirming the contribution of ferroptosis to Hcy/Glu-induced hepatotoxicity. Additional investigations revealed that VPA promotes Hcy accumulation by downregulating its catabolic enzymes (MTR, CBS, CTH), while enhancing Glu accumulation through upregulation of its synthetic enzymes (ALDH4A1, GLS) and repression of the catabolic enzyme GLUL, both in vivo and in vitro. The alterations in MTR, CBS, ALDH4A1, and GLS levels were shown to depend on HDAC1, as demonstrated using HDAC1 knockdown and overexpression systems in HepG2 cells. In summary, VPA disrupts Hcy/Glu homeostasis via HDAC1, leading to ferroptosis and subsequent hepatic steatosis. These findings highlight the HDAC1-Hcy/Glu-ferroptosis axis as a promising therapeutic target for mitigating VPA-induced hepatotoxicity. - Source: PubMed
Publication date: 2026/04/28
Yan XinruiMa LinfengRen JingChen BinyanSong WenxuanDong YuLi XiaojiaoGuo Yingjie - This study synthesized a series of C2 and N1-substituted benzimidazole hydroxamic acid (6-19) as HDAC inhibitors. Among them, most of 2-aryl(alkyl)benzimidazole hydroxamic acids (11-16) exhibited HDAC6 activity and slight HDAC1 (or HDAC2) activity. In addition, they also showed anti-angiogenic activity and inhibited the growth of tested cancer cells. For instance, compound 13 has a GI of 3.9 μM against EPCs and inhibited the growth of HCT-116, SK-Hep-1, and PC-3 cells with GI values of 1.3, 4.2, and 7.5 μM, respectively. The exact mechanism underlying the anti-angiogenic effects of these compounds remains unknown, though this study gives an insight into how future HDAC inhibitors that aim to target blood vessel formation can be designed. - Source: PubMed
Liu Yi-TingLai Cheng-TaWang Shih-WeiLiu Shan-ChiHwang Yi-LinTsai Yi-ChenLee Chi-YehLai Yu-WeiYen Juei-YuWang Po-ChuanLee Hsueh-Yun - Histone deacetylases (HDACs) have been identified as a class of crucial epigenetic enzymes that are responsible for the removal of acetyl groups from the lysine residues in the amino-terminal tails of histones. Their overexpression is closely associated with cancer growth, progression, and acquisition of therapeutic resistance, etc. Therefore, the treatment of diverse cancers could benefit from HDACs inhibitors, especially hematologic malignancies. Herein, a series of novel hydroxamate derivatives were designed by incorporating a clover-leaf scaffold into the cap region of SAHA to explore additional binding sites and obtain more potent HDACs inhibitors. Modifications on cap region and linker led to the optimal inhibitor 31a. Preliminary evaluation of inhibitory potency against HDAC isoenzymes indicated that it could inhibit several HDAC subtypes, including HDAC1 (IC = 2.4 nM), HDAC2 (IC = 5.8 nM), HDAC3 (IC = 5.2 nM), and HDAC6 (IC = 3.3 nM). Additionally, it displayed moderate to potent in vitro antiproliferative activity against broad spectrum of cancers, especially MV4-11 cells (IC = 0.17 μM). Flow cytometry analysis showed that it could induce remarkable cell apoptosis at the concentration of 3.0 μM. However, no cell cycle arrest was observed at the test concentration. Importantly, novel binding sites which could enhance binding affinity with HDAC1 were first confirmed in this work. In our opinion, they are worth applying in the development of HDACs inhibitors. Overall, this study provides a new structure design for HDACs inhibitors and also offers promising novel HDACs inhibitors with potential antiproliferative activity against several types of cancers. - Source: PubMed
Publication date: 2026/04/22
Quan XizhengChen YumeiMa FangliNi YudieQi Baohui - Human RNA polymerase II (Pol II) regulates transcription of significant number of snRNA and proliferation-related mRNA genes by involving Little Elongation Complex (LEC) and Super Elongation Complex (SEC) respectively. However, underlying mechanisms of these differential involvements of Pol II are not known. In this study, we show that human ELL, through its dynamic differential association within LEC and SEC, controls expression of target snRNA and proliferation-related mRNA genes by regulating Pol II recruitment. Mechanistically, we show that p300-mediated acetylation of Lysine 355 (K355) residue favors ELL monomerization and corresponding ELL•SEC formation and proliferation-related mRNA transcription; and reciprocally, HDAC1-mediated deacetylation favors dimerization and subsequent ELL●LEC formation and snRNA transcription; and vice versa. Physiologically, we show that whereas, mitogen treatment enhances AKT signaling-dependent p300-mediated ELL(K355) acetylation leading to increased ELL●SEC assembly and corresponding proliferation-related mRNA transcription, genotoxic stress causes ATM-mediated ELL phosphorylation-dependent deacetylation of ELL(K355) by Sin3A●HDAC1 complex causing enhanced ELL●LEC assembly and snRNA transcription. - Source: PubMed
Publication date: 2026/04/27
Nandy ArijitDalui SambitTalukdar PrathamaChakraborty PoushaliBhagat GauravMinhas Ekjot KaurRoy SrerupaLahiri AbhishakeBasrur VenkateshaBiswas Debabrata