Human HDAC1, Human Blocking Peptide
- Known as:
- Human HDAC1, Human Blocking Peptide
- Catalog number:
- x1876b
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Exalpha
- Gene target:
- Human HDAC1 Blocking Peptide
Related genes to: Human HDAC1, Human Blocking Peptide
- 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: Human HDAC1, Human Blocking Peptide
Related articles to: Human HDAC1, Human Blocking Peptide
- Histone deacetylase 1 (HDAC1) is frequently dysregulated in various human malignancies; however, the molecular mechanisms underlying its role in non‑small cell lung cancer (NSCLC) remain unclear. HDAC1 expression was evaluated in 157 paired lung adenocarcinoma (LUAD) and adjacent non‑neoplastic tissues using tissue microarray and immunohistochemical analysis. The functional role of HDAC1 was assessed in A549, H1299 and H1975 NSCLC cells following stable knockdown or overexpression, using Cell Counting Kit‑8, colony formation and Transwell assays. Downstream signaling was examined by western blotting and nuclear‑cytoplasmic fractionation. Rescue experiments were performed by overexpressing β‑catenin in HDAC1‑knockdown cells and the findings were further validated in a subcutaneous xenograft tumor model in nude mice. HDAC1 was markedly upregulated in LUAD tissues and associated with lymph node metastasis and poor differentiation. Functionally, HDAC1 knockdown inhibited proliferation, colony formation, migration and invasion in all three NSCLC cell lines. These effects were accompanied by downregulation of c‑Myc, cyclin D1 and vimentin, upregulation of E‑cadherin and reduced nuclear β‑catenin accumulation. Conversely, HDAC1 overexpression enhanced malignant phenotypes and promoted β‑catenin nuclear accumulation. Notably, the phosphorylation of AKT (Thr308 and Ser473) and ERK1/2 remained unaltered following HDAC1 modulation. β‑catenin overexpression effectively eliminated the tumor‑suppressive effects of HDAC1 knockdown both and . These findings indicated that HDAC1 is a critical promoter of LUAD progression, acting at least in part through β‑catenin nuclear accumulation. This provided a mechanistic rationale for targeting the HDAC1/β‑catenin axis as a potential epigenetic therapeutic strategy in LUAD. - Source: PubMed
Publication date: 2026/08/14
Xu ShijieChang XiaoluWu XiayuWang FabaoXiang JingLin ChaoxiangZhao HeLi JunzheXu Xianhua - Dual FLT3/HDAC inhibition represents a promising synergistic strategy to address tumor heterogeneity. Building upon our prior lead , we developed novel 6-ethylpyrazine-2-carboxamide derivatives systematic structural optimization to enhance pharmacokinetic properties and target selectivity. The optimized compound, CF-2-17, demonstrated potent dual inhibition of FLT3 (IC = 1.1 nmol/L) and HDACs (IC = 9.6 nmol/L), and exhibited a 27-fold selectivity for HDAC1 over HDAC6. Its improved physicochemical properties, including enhanced solubility and metabolic stability, translated into favorable plasma exposure . In the MOLM-13 (FLT3-ITD) xenograft model, oral administration of CF-2-17 showed antitumor efficacy comparable to combination therapy, without observable toxicity. CF-2-17 also exhibited antiproliferative activity against non-FLT3-ITD hematological malignancies and solid tumors, outperforming single-target agents. Furthermore, CF-2-17 effectively remodeled the tumor immune microenvironment through CD4 T cell activation and IFN- elevation, achieving 87% tumor growth inhibition in LLC syngeneic models. Mechanistically, CF-2-17 reversed FLT3 blockade-induced DC dysfunction activation of the NF-B pathway, thereby reinstating DC-mediated antitumor immunity. This dual FLT3/HDAC inhibitor demonstrates synergistic epigenetic-immune modulation, offering a promising approach for heterogeneous malignancies. - Source: PubMed
Publication date: 2026/05/26
Chang YingjieLi XueWang HuiruiZhao HuajunZhou YueBi WenchaoCheng RuixueShi YuxinWeng HeYang XinyingZhao WeiFang HaoHou Xuben - Histone deacetylases (HDACs) act as transcriptional repressors and play essential roles in mammalian development. However, data on the expression and subcellular localization of HDACs in the tongue and oral mucosa remain limited. This study aimed to investigate the spatiotemporal expression patterns of HDACs in the mouse tongue and oral mucosa during postnatal development and aging. - Source: PubMed
Publication date: 2026/08/12
Yang ChuboWang JingruWang MingxingLi HuishuKong JiaqiGuo XinruZhan Yuanbo - The development of dual inhibitors of histone deacetylases (HDACs) and enhancer of zeste homologue 2 (EZH2) is an efficient strategy that not only synergistically suppresses critical pathways in tumorigenesis but also circumvents the potential risks of drug cocktails. In this study, a series of pyridone derivatives were rationally designed pharmacophore merging, and -((4,6-dimethyl-2-oxo-1,2-dihydropyridin-3-yl)methyl)- -hydroxyoctanediamide (15c) was identified as the most potent compound against hematological tumor cells MV4-11 and SU-DHL-10, with IC values in the submicromolar range. 15c also effectively inhibited HDAC1 and EZH2 with IC values of 9.2 nM and 311.1 nM, respectively. Molecular simulations revealed key interactions between 15c and both targets. These findings indicated that compound 15c warrants further investigation as a novel dual HDAC/EZH2 agent. - Source: PubMed
Publication date: 2026/08/11
Tan ZhaobangDing JiajunChen XinQian LeiYu Qiang - Nonalcoholic fatty liver disease (NAFLD) is characterized by profound metabolic reprogramming. Recent evidence suggests that lactate, beyond its role as a metabolic waste product, may modulate histone lactylation, linking metabolic stress to the epigenetic regulation of disease progression. However, the specific lactate-related gene (LRG) signatures driving NAFLD remain to be elucidated. - Source: PubMed
Publication date: 2026/08/07
He QingxuanWang XuWang PengfeiZhao QiweiLiu DonglinLuo YueGuo Feng-YiLiu ZiyuYang Xiao