TGM2 antibody
- Known as:
- TGM2 (anti-)
- Catalog number:
- orb101298
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- TGM2 antibody
Related genes to: TGM2 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 antibody
Related articles to: TGM2 antibody
- Obesity, a chronic metabolic disease, lacks effective treatments. Intermittent fasting (IF), especially time-restricted feeding (TRF), shows promise, yet the comparative molecular effects of different regimens remain unclear. This study examined their impact on 3T3-L1 adipocytes and transcriptomic changes. - Source: PubMed
Publication date: 2026/03/14
Er Pei HanChye Jin YiLetchumanan GeethaSay Yee-How - Irradiation (IR) can cause intestinal epithelial cell death, damage to crypt stem cells, and mucosal barrier dysfunction, which are the features of radiation-induced intestinal injury (RIII). Our study first discovered a natural small-molecule alkaloid D (OV16) with an obvious radiation protection effect. This study aims to investigate the radiation protection effect of OV16 on RIII and its potential molecular mechanism. The results showed that in vitro OV16 exhibited a significant protective effect on an irradiated human small intestinal epithelial cell-6 (HIEC-6) model. Then, transglutaminase 2 (TGM2), which is the key protein for OV16 to exert its anti-RIII protective effect, was identified as a crucial cellular target of OV16 using drug affinity responsive target stability (DARTS), molecular docking, molecular dynamics simulation, cell thermal shift assay (CETSA), and microscale thermophoresis (MST). Moreover, OV16 can upregulate the expression level of TGM2 in the nucleus of HIEC-6. TGM2 can reduce radiation-induced damage by enhancing the proliferation ability and migration ability of HIEC-6 and reducing the generation of γ-H2AX. Collectively, our study first identified TGM2 as a previously unreported therapeutic target for RIII, and provided a future drug design direction for TGM2 allosteric activators using OV16 as a novel molecular template. - Source: PubMed
Publication date: 2026/06/05
Zhang ZhiyanWang HeCui YaowenLu YangXu YingyingLi MinLiu SifanTian YingXia ZimingZhang GuangjieLiu Shuchen - Histaminylation is a newly discovered monoaminylation catalyzed by transglutaminase 2 (TGM2), and its role in myocardial fibrosis has not yet been elucidated. Here, we identified histaminylation in cardiac type I collagen isolated from mice 7 days after acute myocardial infarction (AMI) by mass spectrometry. Using histamine-deficient Hdc mice, we demonstrated an increase in TGM2-mediated γ-glutamyl-ε-lysine crosslinks and a higher myocardial Young's modulus in the scar region of Hdc mice than in wild-type controls, indicating that histaminylation might restrain the role of TGM2 in cardiac fibrogenesis after AMI. Furthermore, we reconstituted an in vitro crosslinking system, yielding unmodified collagen and histaminylated collagen. The results of mechanical indentation and electron microscopy demonstrated that histaminylation could reduce crosslink formation, lower matrix stiffness, and alter viscoelasticity. Subsequently, primary murine cardiac fibroblasts were cultured under cyclic stretch with TGF-β on different substrates, and the results revealed that histaminylated collagen strongly attenuated TGF-β-induced fibroblast-to-myofibroblast transition and reduced focal adhesion assembly. Mechanically, integrated single-cell and bulk RNA-seq analyses indicated that the PIEZO1/ITGB1 mechanotransduction axis was upregulated and mediated downstream signal transduction in the infarcted hearts of Hdc mice. Finally, local delivery of a histamine-releasing hydrogel to Hdc mice after AMI could significantly reinstate collagen histaminylation and reduce crosslink abundance and cardiac dysfunction. Collectively, these data reveal that collagen histaminylation limits TGM2-dependent crosslinking, softens the extracellular matrix, and inhibits the PIEZO1/ITGB1 axis, thereby mitigating myocardial fibrosis after AMI. This study also highlights a novel role of histamine in maintaining stress environment mechanical stability. - Source: PubMed
Publication date: 2026/06/11
Zhu JianfuSun DiliZeng GaofengWu KehanYang XiyangZhu XiaoweiAierken DiyaerjiangDing SulingWang XiangfeiGe JunboYang Xiangdong - Osteosarcoma has a poor prognosis and frequently metastasizes to the lungs. This study examined the role of transglutaminase 2 (TGM2), a ligand for adhesion G protein-coupled receptor 56 (GPR56), in lung metastasis of LM8 mouse osteosarcoma cells. Gβγ‑dependent ERK signaling mediated by GPR56 and the adhesion of GPR56-expressing LM8 cells and GPR56‑deficient LM8 cells were analyzed using siRNA, western blotting, and cell staining. TGM2 and Ki67 expression in metastatic lung lesions was assessed by transplantation and immunohistochemistry. TGM2 enhanced endogenous ERK signaling in LM8 cells. In the absence of TGM2, ERK signaling increased in LM8 cells but remained unchanged in LM8 cells compared with LM8 cells. In the presence of TGM2, ERK activity in LM8 cells resembled LM8, whereas it was decreased in LM8 cells. LM8 cells showed reduced adhesion, whereas LM8 cells did not differ from LM8 cells. Proliferation did not differ between LM8 cells and LM8 cells. TGM2 was co‑expressed in CD31 + endothelial cells, and Ki67‑positive LM8 cells were observed along bronchi. These findings suggest that GPR56 promotes lung metastasis through TGM2‑mediated adhesion to pulmonary endothelial cells and enhanced ERK‑dependent proliferative signaling. - Source: PubMed
Publication date: 2026/06/10
Suzuki NobuyoshiHayakawa ErikaNishiura HiroshiChen WentingImasaka MaiSugimoto MichihikoTachibana ToshiyaOhmuraya Masaki - An imbalance in M1/M2 macrophage polarization has been shown to play a critical role in the pathogenesis of diffuse alveolar hemorrhage (DAH) in mouse models. However, its contribution to immune-associated DAH in humans remains unclear. This study aimed to investigate the role of macrophage M1/M2 polarization imbalance in the pathogenesis of immune-associated DAH in children. - Source: PubMed
Wei QingChen XunLu FuceDeng YanLiu JingLi YanNong Guangmin