HDAC4 Antibody
- Known as:
- HDAC4 Antibody
- Catalog number:
- abx000624
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- HDAC4 Antibody
Related genes to: HDAC4 Antibody
- Gene:
- HDAC4 NIH gene
- Name:
- histone deacetylase 4
- Previous symbol:
- BDMR
- Synonyms:
- KIAA0288, HDAC-A, HDACA, HD4, HA6116, HDAC-4
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-11-28
- Date modifiied:
- 2015-09-11
Related products to: HDAC4 Antibody
Related articles to: HDAC4 Antibody
- Epigenetic dysregulation plays a critical role in tumorigenesis and cancer progression. The development of isoform-selective histone deacetylase (HDAC) inhibitors has emerged as a promising strategy in cancer therapy. In this study, based on our previously identified hit compounds, a series of novel N-arylamide-quinoline derivatives were rationally designed and synthesized as HDAC isoform-selective inhibitors with improved efficacy and reduced toxicity. Among them, 6b exhibited potent inhibitory activity against HDAC1, 2, 3, and 10, while showing no activity against HDAC4-9, a selectivity profile further supported by molecular docking and molecular dynamics simulation. 6b demonstrated significant antiproliferative effects against HL-60, CCRF-CEM, and HepG2 cancer cells. In vitro toxicity assays revealed a high selectivity index for this compound, markedly superior to that of the parent compounds. Mechanistic studies showed that it induced hyperacetylation of histone H3 in a concentration-dependent manner, downregulated Rb protein and caspase-8 precursor, and modulated the expression of BAX, BAK, and BCL-2, leading to extrinsic apoptosis and G/G phase cell cycle arrest. In vivo, 6b exhibited potent antitumor activity with no apparent toxicity following both intragastric administration and intraperitoneal injection. Notably, intraperitoneal delivery resulted in enhanced efficacy. Pharmacokinetic studies further characterized the in vivo behavior of this compound via both routes. Overall, hit compound 6b displays favorable biological properties and represents a promising candidate for further anticancer drug development, with subsequent studies focusing on the optimization of its drug-like properties. - Source: PubMed
Publication date: 2026/04/13
Yu BingyanWang NingLou GaojieWu LingjieWang YuleYin SijiaLu YiXu JunWang ZeChen XinyuanHe ShanZhang Bin - Body size traits serve as crucial phenotypic indicators of body conformation and growth, showing a close correlation with production performance. To elucidate the genetic basis of these traits and identify potential molecular markers in Saanen dairy goats, we analyzed low-coverage whole-genome sequencing (lcWGS) data from 635 individuals. Following genotype imputation based on an in-house goat reference panel, we obtained 14 million single-nucleotide polymorphisms (SNPs) and 45 thousand structural variants (SVs). Genetic parameters were estimated using SNP data. Subsequently, single-trait (ST) and multi-trait genome-wide association studies (MT-GWAS) were conducted using both SNP and SV datasets. Results indicated that body height, body length, and rump height possess moderate heritability, with positive genetic and phenotypic correlations observed among these traits. ST-GWAS identified 56 significant SNPs and 3 significant SVs, mapping to 30 candidate genes, including , , and . Furthermore, MT-GWAS detected 2 significant SNPs and 2 significant SVs missed by ST-GWAS, identifying 4 additional candidate genes (, , , and ). Notably, overlapping association signals for body length and rump height were observed near on chromosome 10, with colocalization analysis supporting the existence of a shared causal variant in this region. KEGG enrichment analysis indicated that candidate genes were primarily enriched in fatty acid biosynthesis and related metabolic pathways. In conclusion, this study shows that integrating structural variants into MT-GWAS can reveal association signals beyond those captured by SNPs, providing a theoretical basis for marker-assisted selection and precision breeding for body conformation. - Source: PubMed
Feng Yan-ShuaiLi Jia-XinZhao Jiong-YaoCao Jia-leWang Xing-QuanYao XiaotingFu Ji-AqiWang Xi-Hong - - Source: PubMed
Publication date: 2026/04/15
Mishra SujataA Sai Ananya PavaniVema AparnaKalle Arunasree M - Multiple myeloma (MM) is a plasma cell malignancy that originates in the bone marrow (BM) and is characterized by the clonal expansion of Bcell-derived plasma cells producing abnormal monoclonal immunoglobulins. Despite significant therapeutic advances that have improved patient outcomes, drug resistance remains a major obstacle to effective disease management. Genetic and epigenetic heterogeneity are key features of MM that drive disease onset, progression, and therapeutic resistance. Both early and advanced stages of MM exhibit global and locus specific DNA methylation abnormalities that silence tumor suppressor genes and disrupt key regulatory pathways, including Wnt/β-catenin, JAK/STAT, and apoptotic signaling. Altered activity of histone modifiers, including methyltransferases (e.g., EZH2, MMSET) and deacetylases (e.g., HDAC4, HDAC6), promotes chromatin remodeling and myeloma cell survival, representing promising therapeutic targets. Dysregulated long non-coding RNAs (lncRNAs), such as MALAT1 and MIAT1, further contribute to genomic instability and drug resistance. Emerging epigenetic therapies targeting DNA methyltransferases, HDACs, and bromodomains show promise in overcoming therapeutic resistance and improving patient outcomes. In this article, we summarize current insights into the central role of epigenetic alterations including DNA methylation changes, histone post-translational modifications, and lncRNA dysregulation in MM pathogenesis, discuss their mechanistic and clinical implications, and highlight therapeutic opportunities emerging from these discoveries. - Source: PubMed
Publication date: 2026/04/09
Alipoor Shamila DShrestha MariuszLiu AijunChang Hong - Phosphorylation of Thr221 (T221) in salt-inducible kinase 3 (SIK3) is a key determinant of its catalytic activity, with broad implications ranging from sleep homeostasis to tumorigenesis. Despite its physiological significance, however, the underlying molecular mechanism by which this phosphorylation event regulates enzymatic activity remains poorly understood. Here, we combine all-atom molecular dynamics (MD) simulations, quantum mechanics/molecular mechanics (QM/MM)-based steered molecular dynamics (SMD) simulations, molecular mechanics/generalized Born surface area (MM/GBSA) binding free-energy calculations, protein contact network (PCN) analysis, and principal component analysis (PCA) to systematically elucidate the allosteric effects of T221 phosphorylation. We show that a highly occupied pT221-Arg112 salt bridge stabilizes the αC-helix in its "in" conformation and strengthens the conserved Glu113(αC-helix)-Lys95(β3-strand) interaction, thereby biasing the conformational ensemble toward active-like states. This inward orientation of the αC-helix, directed toward both the ATP-binding pocket and the catalytic center, further positions Lys109 to maintain a persistent and energetically favorable salt bridge with ATP, consistent with enhanced ATP affinity. Consistent with these atomistic observations, PCA and MM/GBSA analyses reveal a phosphorylation-induced population shift toward a lower free-energy ensemble and substantially stronger ATP binding, jointly indicating a coordinated allosteric enhancement of catalytic activity. Further QM/MM MD simulations indicate that T221 phosphorylation pre-organizes the SIK3 active site to position HDAC4-Ser245(Oγ) closer to the ATP γ-phosphate in a reaction-competent arrangement, thereby facilitating Ser245-O-P phosphoester bond formation and promoting Ser245 phosphorylation. Taken together, these findings define-at atomic resolution-the detailed structural and dynamic principles by which T221 phosphorylation regulates SIK3 function, thus providing mechanistic insight into sleep-need homeostasis and offering a foundation for structure-guided development of SIK3-targeted cancer therapeutics. - Source: PubMed
Publication date: 2026/04/08
Wang ShuoZhang YaoyueZhang YujieWang ZhihuiYao XiaoningGong LidongLi GuohuiWang Anhui