TGM2 Mouse Monoclonal Antibody
- Known as:
- TGM2 Mouse Monoclonal Antibody
- Catalog number:
- ENZ-007052-M10
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- TGM2 Mouse Monoclonal Antibody
Related genes to: TGM2 Mouse Monoclonal Antibody
- Gene:
- TGM2 NIH gene
- Name:
- transglutaminase 2
- Previous symbol:
- -
- Synonyms:
- TGC
- Chromosome:
- 20q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-08-02
- Date modifiied:
- 2016-10-05
Related products to: TGM2 Mouse Monoclonal Antibody
Related articles to: TGM2 Mouse Monoclonal Antibody
- Monoamine neurotransmitters dopamine and 5-hydroxytryptamine (serotonin, 5-HT), traditionally implicated in the central nervous system, are increasingly recognized as contributors to hepatocellular carcinoma (HCC). However, the underlying molecular mechanisms remain unclear. Here, we demonstrate that the E3 ubiquitin ligase F-box-only protein 6 (FBXO6) is highly expressed in HCC patients. FBXO6 promotes accumulation of 5-HT and dopamine in HCC by mediating K48-linked ubiquitination and degradation of monoamine oxidase A (MAOA). Elevated monoamine levels activate their cognate receptors, triggering the PI3K/AKT/mTOR signaling axis. Simultaneously, these neurotransmitters induce transglutaminase 2 (TGM2)-dependent histone monoaminylation (H3Q5ser and H3Q5dop), forming a synergistic oncogenic circuit that drives HCC development. Clinical specimens reveal a strong inverse correlation between FBXO6 and MAOA protein levels, validating this regulatory axis. Preclinical studies demonstrate that combined treatment with the mTOR inhibitor everolimus and the TGM2 inhibitor GK921 exerts synergistic antitumor effects against FBXO6-driven HCC, providing a rational therapeutic strategy for patients with FBXO6 overexpression. - Source: PubMed
Publication date: 2026/08/17
Li ChunmingZhang YujunLin Xiao-TongZhang JieZhang Lei-DaGong JianpingXie Chuan-Ming - Histamine is a key signaling molecule in pathophysiology that can exhibit significant regulatory roles in diverse health and disease states. Besides the well-studied noncovalent interactions between histamine and its receptors, protein histaminylation is a recently discovered mechanism of action through which histamine regulates cellular signaling pathways in a covalent modification manner. Histaminylation is an emerging protein post-translational modification (PTM), where an isopeptide bond is formed between the histamine primary amine and the γ-carboxyl group of glutamine through a transamidation reaction catalyzed by transglutaminase 2 (TGM2). However, due to the lack of efficient pan-specific antibodies targeting histaminylated glutamine, the histaminylation proteome in cells remains poorly explored. Here, we report the design and development of a novel Nτ-propargylated histamine (Nτ-PH) probe as well as its successful application in chemical proteomic profiling of the histaminylation proteome in cancer cells. Notably, new TGM2-catalyzed epigenetic marks on core histones, e.g., H2AX-Q84 and Q104 histaminylation, have been identified from cancer cells and verified. Lastly, the crosstalk between H2AX histaminylation and γH2AX formation was discovered in this study, suggesting that TGM2-mediated histaminylation plays a critical role in DNA damage responses. - Source: PubMed
Ma XingyuLeaman Anne ALin ZengLi HuapengCai ZhengjunWang QianyueDalal KaiwaanHossain Md ShahadatThirumalaikumar Venkatesh PWang ZhihongO'Brien Valerie PTao W AndyZheng Qingfei - Idiopathic pulmonary fibrosis (IPF) is associated with cigarette smoking, yet the relationship between the tobacco-specific nitrosamine nicotine-derived nitrosamine ketone (NNK) and IPF-associated lung transcriptional remodeling remains incompletely understood. Here, we developed an exposure-informed computational framework integrating multi-database target prediction, lung single-cell and single-nucleus transcriptomic analysis, co-expression network analysis, bulk lung cohort projection, and exploratory structure-based modeling. Putative human protein targets of NNK were predicted from ChEMBL, PharmMapper, and SwissTargetPrediction, yielding 2,505 nonredundant targets. These targets were intersected with IPF-associated intramodular hub genes identified from cell type-specific weighted gene co-expression network analysis, defining a focused 42-gene ExposureA-core gene set. Projected ExposureA-core scores showed the clearest IPF-control differences in endothelial and epithelial pseudo-bulk profiles. Functional annotation of the training-derived epithelial ExposureA-core Top30 signature highlighted MAPK and p38 MAPK signaling, PI3K-AKT signaling, angiogenesis or vasculature regulation, cell-substrate adhesion, and membrane-, adhesion-, and cytoskeleton-related cellular components, suggesting remodeling- and adhesion-related epithelial transcriptional features in IPF. The fixed epithelial ExposureA-core Top30 signature remained detectable in independent bulk lung transcriptomic cohorts without gene re-selection, coefficient fitting, or score optimization, with exploratory ROC analyses showing apparent IPF-control separation in GSE110147 and GSE92592. Exploratory docking and 100-ns molecular dynamics simulations of selected epithelial Top30-encoded candidates showed that modeled ECE1-NNK, MMP7-NNK, and TGM2-NNK complexes reached dynamic equilibrium, with relatively stable RMSD, radius of gyration, solvent-accessible surface area, residue-level fluctuation, and low-energy conformational states, supporting their structural plausibility as candidate modeled complexes. Overall, this study defines a focused exposure-informed IPF-associated transcriptional framework and prioritizes epithelial remodeling-related candidate features for future experimental validation. These findings support hypothesis-generating computational prioritization rather than direct evidence that NNK drives IPF pathogenesis. - Source: PubMed
Publication date: 2026/07/31
Meng KairuiWang LuGong XueqingTang WenjunJia GuobingWang YanmeiHe Chengshi - Type 2 inflammation (T2I) drives chronic airway diseases such as eosinophilic chronic rhinosinusitis (eCRS) and asthma, which are frequently accompanied by coagulation activation and platelet recruitment. However, whether and how these associated processes actively contribute to shaping inflammation remain largely unknown. Here, using single-cell transcriptomic profiling of human nasal polyp samples from eCRS patients with or without comorbid asthma, we identified a TGM2 macrophage population enriched in inflamed tissues and strongly correlated with local eosinophilia and systemic disease burden. Using dust mite-induced type 2 airway inflammation models in mice, we showed that the loss of Tgm2, either globally or in macrophages, selectively impaired alternative macrophage activation and attenuated both eosinophilic inflammation and epithelial remodeling. Mechanistically, TGM2 catalyzes the recently described histone modification H3Q5 serotonylation (H3Q5Ser), promoting an epigenetically permissive chromatin state for alternative macrophage activation. We further revealed a transcellular circuit driven by the activated platelet-derived monoamine metabolite serotonin (5-HT), which acts as a critical paracrine signal to fuel this epigenetic reprogramming of macrophages. Crucially, pharmacological inhibition of platelet 5-HT release or TGM2 activity ameliorated both nasal and pulmonary pathology in a mouse model of type 2 inflammation, underscoring the therapeutic potential of this pathway. Our findings establish a serotonin-TGM2-H3Q5Ser axis that couples platelet activation to macrophage epigenetic programming. This transcellular mechanism drives type 2 inflammation and reveals novel therapeutic opportunities across airway diseases. - Source: PubMed
Publication date: 2026/07/30
Tang RuXia GuofangZhu YingSheng JinhongLiu ZhihanMao SongZhou JiayaoGu YuelongPu ShileiLi ZhipengLin HaiXu CongfengXu HongqingZhang FengZhao YongxuYin ShankaiZhang WeitianLiu Feng - As a short-chain fatty acid and histone deacetylase (HDAC) inhibitor, butyrate possesses extensive immunomodulatory properties. Here, we uncover a novel mechanism wherein butyrate markedly upregulates the expression of the immune checkpoint PD-L1 across diverse tumor cell types. Mechanistically, epigenetic analyses revealed that butyrate drives PD-L1 transcriptional activation through dual synergistic pathways: increasing histone H3 acetylation (H3Ac) at the promoter via HDAC inhibition, and enhancing histone H3K4me3 modification by upregulating transglutaminase 2 (TGM2). Combining butyrate or high-fiber diets with anti-PD-L1 antibodies profoundly suppressed tumor growth and bolstered anti-tumor immunity in both subcutaneous and AOM-DSS-induced colorectal cancer (CRC) murine models. Ultimately, our results highlight butyrate and dietary fiber supplementation as promising sensitizing strategies to augment the efficacy of PD-L1 blockade in patients with low baseline PD-L1 expression. - Source: PubMed
Publication date: 2026/07/20
Sun XueGao YiLi JiaxiMa YanLi HongchenWang ZhenLv LeiXu Yanping