Mouse Histone deacetylase 11,HDAC11 ELISA KIT
- Known as:
- Mouse Histone deacetylase 11,HDAC11 Enzyme-linked immunosorbent assay test KIT
- Catalog number:
- E1115Mo
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- Sunlog
- Gene target:
- Mouse Histone deacetylase 11 HDAC11 ELISA KIT
Related genes to: Mouse Histone deacetylase 11,HDAC11 ELISA KIT
- Gene:
- HDAC11 NIH gene
- Name:
- histone deacetylase 11
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-09
- Date modifiied:
- 2014-11-19
Related products to: Mouse Histone deacetylase 11,HDAC11 ELISA KIT
Related articles to: Mouse Histone deacetylase 11,HDAC11 ELISA KIT
- Staphylococcus aureus is a facultative intracellular pathogen that persists within both professional and non-professional phagocytes, contributing to chronic and antibiotic-resistant infections. Autophagy, particularly xenophagy, serves as a central cell-autonomous defense pathway that can capture intracellular S. aureus and deliver it to lysosomes for degradation. However, the bacterium has evolved multiple strategies to subvert xenophagic clearance, including manipulation of bacteria-containing autophagosome maturation, blockade of autophagosome and lysosome fusion, and co-option of autophagy-related machinery to create intracellular survival niches. Recent studies have also identified host pathways that shape infection outcomes, including reprogramming of cell death cascades to simultaneously sustain host viability and suppress xenophagy, and co-option of mitophagy to eliminate bactericidal mitochondrial ROS. As illustrative examples, caspase-8 reprogramming uncouples host survival from effective xenophagy, and the HDAC11/IL10/mTOR/PINK1-PRKN axis drives mitophagy to suppress mitochondrial ROS. We further address the largely unexplored roles of chaperone-mediated autophagy and endosomal microautophagy in S. aureus infection, drawing on mechanistic paradigms from viral and mycobacterial infections. Since S. aureus can impair autophagosome maturation, lysosomal acidification, and fusion between bacteria-containing autophagosomes and lysosomes, enhancing autophagy initiation alone may not always translate into improved bacterial clearance. We therefore propose, as a testable hypothesis, that host-directed strategies aimed at restoring lysosomal competence, improving degradative flux, or neutralizing bacterial virulence mechanisms may complement or outperform upstream autophagy induction in selected infection contexts. However, this concept remains insufficiently validated, and direct comparative studies in relevant host cell types and animal models are needed before lysosome-directed approaches can be prioritized therapeutically. - Source: PubMed
Publication date: 2026/07/28
Hu PengLu MingyaoN'San Hillary CassandreChen PingLiu HuiyuShi Yong - Inspired by reports that HDAC blockade can trigger compensatory activation of the LIFR-JAK1-STAT3 axis in solid tumors, we designed and synthesized a series of niclosamide-based STAT3/HDAC dual-target inhibitor candidates by incorporating a SAHA-derived hydroxamate zinc-binding group into the pleiotropic, STAT3-modulating niclosamide scaffold. Biological evaluation identified NS06 as the best-balanced analogue, with IC values of 1.49 and 1.41 μM against MDA-MB-231 and HCT116 cells, respectively. Mechanistic studies showed that NS06 bound STAT3 in vitro (SPR, K = 5.82 μM), suppressed STAT3 phosphorylation, and inhibited HDAC1, HDAC3, and HDAC6 with IC values of 129.1, 451.2, and 230.4 nM, respectively, while showing limited inhibition of HDAC4 and HDAC11 in the primary screen. NS06 also increased histone H3 acetylation, induced apoptosis, and inhibited migration and colony formation. In addition, NS06 retained antiproliferative activity in a 3D tumor spheroid model and showed improved Caco-2 permeability together with moderate liver microsomal stability (t ≈ 48.6 min in rat liver microsomes). Docking and 100-ns molecular dynamics simulations further supported chemically plausible binding modes in the HDAC1 catalytic pocket and the STAT3 SH2 domain. Overall, these findings support niclosamide as a tractable scaffold for mechanism-driven STAT3/HDAC dual-target inhibitor design and identify NS06 as a promising lead for further optimization against solid tumors. - Source: PubMed
Publication date: 2026/07/25
Shi YuchenZhang QihaoWang ChenxiLu ZipengChen FangfangHan LiuXu ZhouyangZhang YuanMa ShumeiYe FaqingWang Xuebao - Although receptor tyrosine kinase inhibitors (sorafenib and lenvatinib) have been applied as a first-line targeted therapy for advanced unresectable hepatocellular carcinoma (HCC) for decades, their clinical efficacy is limited and the underlying mechanism remains unclear. HCC is a highly glycolytic malignancy characterized by excessive lactate accumulation in the tumor microenvironment (TME). Emerging evidences show that histone lactylation plays a critical role in various biological processes, but its function in receptor tyrosine kinase inhibitor resistance remains obscure. This study was designed to elucidate the role of histone lactylation in receptor tyrosine kinase inhibitor resistance in HCC. Clinical cohort analyses revealed that the increased nuclear pan-lysine lactylation (pan-Kla) predicts poor patient prognosis and high H4K12la level correlates with targeted drug resistance. Furthermore, lactate bidirectionally controls H4K12la through the opposing enzymatic activities of AARS1 (writer) and HDAC11 (eraser). Integrative CUT&Tag and ATAC-seq analyses demonstrated that H4K12la directly activates the promoter of RAPGEF3, a predominant upstream regulator of the RAP1 signaling pathway. Inhibition of RAPGEF3 reversed the lactate-induced targeted drug resistance both in vitro and in vivo, suggesting H4K12 lactylation modulates targeted drug resistance by activating RAPGEF3-RAP1 signaling. Notably, combining the RAPGEF3 inhibitor ESI-09 with lenvatinib synergistically suppressed HCC growth in mouse models. Clinico-pathological analyses revealed that elevated expression of the AARS1/H4K12la/RAPGEF3 axis correlated with inferior survival and sorafenib resistance in HCC patients, which was further confirmed in patient-derived xenograft (PDX) models. This study delineates a novel metabolic-epigenetic mechanism whereby lactate modulates hepatocellular carcinoma sensitivity to targeted therapies through histone lactylation and suggests AARS1-H4K12la-RAPGEF3 axis may serve as an interventional target to overcome targeted drug resistance, offering a promising strategy to enhance clinical outcomes in HCC patients. - Source: PubMed
Publication date: 2026/07/21
Zeng TanlunZhu WanwanSun GuanqunWang TengjiaoLiu ChennaHu GuanghuiLiu JunyuLing PengyunWang LiFan ChangLee Terence Kin WahXiao JianruLiang XijunDing Jin - Accurate virtual screening of ultra-large chemical libraries remains challenging. Existing approaches rely on lower-fidelity scoring functions or sampling-based strategies that can limit predictive accuracy and bias the exploration of chemical space. Here, we present FastBindRank, a distillation-based framework that transfers the predictive power of the structure-based model Boltz-2 into an efficient sequence-based surrogate. Trained on ~1% of the 122-million-compound PubChem library, FastBindRank enables high-fidelity screening at scale. Applied to histone deacetylase 11 (HDAC11), FastBindRank substantially enriched high-confidence binders relative to the background chemical space. The lightweight model captured structural patterns associated with predicted binding, revealing structural determinants of binding. Under a comparable computational budget, FastBindRank achieved a 74-fold increase in hit rate and over a 30-fold increase in discovery yield over direct subset-based screening. Experimental validation confirmed the activity of two novel compounds. These results establish distillation as a practical strategy for scalable, high-fidelity virtual screening of ultra-large chemical libraries. - Source: PubMed
Publication date: 2026/07/03
Dai JiaweiWang YueyueShan Naing LinMariani MarcoYu ZimengYan QinGolani Lalit KSurovtseva Yulia VLee William HPusztai Lajos - Epigenetic regulation is indispensable for embryonic development, yet the specific roles of histone deacetylases (HDACs)-a core family of epigenetic regulatory enzymes-in orchestrating craniofacial morphogenesis remain incompletely elucidated. C57BL/6 mouse embryos spanning embryonic Day 12.5 (E12.5) to E16.5 were analyzed. Histological staining (hematoxylin-eosin and Masson staining) was used to characterize morphological development of the tongue, palate, and mandible. Immunohistochemistry (IHC) was performed to map the spatiotemporal expression patterns of HDAC1-11. HDAC1 expression was scarcely detectable throughout the entire E12.5-E16.5 period. In contrast, HDAC2 showed robust expression in the mandible and tongue from E13.5 to E15.5. Notably, HDAC2 also exhibited strong positive staining in palatal epithelial cells at E14.5. By E16.5, HDAC1-10 expression became barely detectable in tongue, palate, and mandible, whereas HDAC11 retained intense expression specifically in the mandible at this late maturation stage. HDAC family members exhibit divergent spatiotemporal expression profiles during craniofacial development, with distinct subtype-specific patterns that align with key stages of tongue, palate and mandible morphogenesis. These findings establish a comprehensive spatiotemporal expression atlas of HDAC1-11 in developing craniofacial organs, providing essential foundational data to guide future investigations into the epigenetic regulation of craniofacial development. - Source: PubMed
Yang ChuboWang MingxingKong JiaqiWang JingruLi HuishuGuo XinruZhan Yuanbo