TIGAR Rabbit Polyclonal Antibody
- Known as:
- TIGAR Rabbit Polyclonal Antibody
- Catalog number:
- APO-4049
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- TIGAR Rabbit Polyclonal Antibody
Related genes to: TIGAR Rabbit Polyclonal Antibody
- Gene:
- TIGAR NIH gene
- Name:
- TP53 induced glycolysis regulatory phosphatase
- Previous symbol:
- C12orf5
- Synonyms:
- -
- Chromosome:
- 12p13.32
- Locus Type:
- gene with protein product
- Date approved:
- 2000-08-24
- Date modifiied:
- 2015-08-13
Related products to: TIGAR Rabbit Polyclonal Antibody
Related articles to: TIGAR Rabbit Polyclonal Antibody
- : Inclusion complexes among drugs and cyclodextrin-modified polymers are a topic of recent interest in pharmaceutical research and industry as they might expand the solubility, bioavailability, and stability of the guest molecules. Polyurethanes derived from cyclodextrins show some biomedical applications. In this study, two cross-linked polyurethane networks based on hydroxypropyl-β-cyclodextrin (HPβCD) and polyethylene glycols (PEG 2000 or PEG 6000) were synthesized with NCO/OH molar ratio 4.3 and 6.3 by the typical two-step polymerization method. : Inclusion complexes of clotrimazole (CLOT) with two HPCD-modified polyurethane networks and their corresponding physical mixtures were prepared using kneading methods and physical mixing in a 1:6 weight ratio of CLOT:HPβCD. : Obtained prepolymers, previously end-capped with isocyanate groups forming urethane links with HPβCD, which were confirmed by FTIR analysis. TGA results indicate a slight increase in thermal stability of the prepared complexes. The characteristic endothermic peak of the CLOT at around 145.90 °C did not appear in the DSC curve of the drug-loaded inclusion complexes. The XRD patterns of physical mixtures showed specific peaks corresponding to pure clotrimazole. SEM micrographs confirmed an elliptical/spherical- and plate-shaped particles without phase segregation, indirectly confirming that CLOT is not separately present due to inclusion into HPβCD and entrapment into polyurethane networks. Novel complexes PUR2/HPβCD-CLOT-IC and PUR3/HPβCD-CLOT-IC were applied as drug carriers, and diffusion-controlled kinetics of CLOT release were best described using Higuchi model. : The obtained in vitro results showed surprisingly slow/prolonged clotrimazole release from modified polyurethane networks due to the significant influence of NCO/OH molar ratio and the chosen polyol soft segments chain length with potential in vivo applications. - Source: PubMed
Publication date: 2026/03/14
Cakić Suzana MIlić-Stojanović Snežana SNikolić Ljubiša BNikolić Vesna DRistić Ivan SMarković Gordana SNikolić Nada Č - This study focused on clarifying whether methyltransferase3 (METTL3) participates in the polarization and activation of microglia in Alzheimer's disease (AD) by mediating the N6-methyladenosine (m6A) modification level of TP53-induced glycolysis and apoptosis regulator (TIGAR). - Source: PubMed
Publication date: 2026/02/25
Kang JingDu XinZhang XiaotingLi YadongWang ChunyingSun Shiming - Oxidative stress and metabolic dysregulation in goblet cells are pivotal in ulcerative colitis (UC) pathogenesis. TIGAR promotes the synthesis of NADPH and contributes to mitigate oxidative stress, but how it regulates NADPH production and affects UC remains unclear. Here we demonstrate that TIGAR inhibits lactylation of the key NADPH-synthesizing enzymes G6PD (at K432) and 6PGD (at K38), thereby preserving their enzymatic activities by promoting G6PD homodimer formation and 6PGD binding to NADP. In male UC mice, persistently low TIGAR expression elevates lactate levels, promoting the lactylation of G6PD and 6PGD and impairing their function. This process suppresses NADPH synthesis, exacerbating goblet cell oxidative stress. The resulting decline in Trx1 reductase activity induces S-nitrosylation of the mucin-processing enzyme AGR2, thereby inhibiting mature MUC2 production and compromising the intestinal mucus barrier. Our findings elucidate a mechanistic pathway through which TIGAR maintains cellular redox homeostasis, presenting it as a potential therapeutic target for UC. - Source: PubMed
Publication date: 2026/03/03
Wu DanSu SenZhang PanyangZha XuleWei YanZhang TingLiu XiaoyanChen QianLi ChunyanHuang QianyingZhou ZhihaoYang YanXia LinFan ShijunPeng Xi - Mitochondrial dysfunction devastates the heart in major cardiovascular diseases, yet the mechanisms governing mitochondrial quality control remain elusive. We discovered that TIGAR (TP53-induced glycolysis and apoptosis regulator) deficiency established profound cardiac protection through developmental epigenetic programming of Parkin expression. Using whole-body and cardiomyocyte-specific TIGAR knockout mice, we demonstrated remarkable cardioprotection following myocardial infarction with maintained ejection fraction, and complete resistance to diet-induced cardiac hypertrophy despite comparable weight gain. TIGAR deficiency triggered dramatic increases in Parkin expression across all somatic tissues except testes, where Parkin levels remained extraordinarily high (100-fold greater than cardiac levels) regardless of TIGAR status, revealing tissue-specific regulatory mechanisms. This protection was entirely Parkin-dependent, as double knockout mice lost all cardioprotective benefits. Crucially, adult TIGAR manipulation failed to alter Parkin levels, demonstrating that this pathway operated exclusively during critical developmental windows to program lifelong cardiac resilience. Whole-genome bisulfite sequencing identified reduced DNA methylation in Prkn intron 10 as the key regulatory mechanism, with CRISPR deletion dramatically increased Parkin expression in multiple cell lines. Our findings reveiled how early cardiac metabolism programmed lifelong cardiac function through epigenetic mechanisms, and identifyied developmental metabolic programming as a potential therapeutic target for preventing both ischemic heart disease and metabolic cardiomyopathy. - Source: PubMed
Publication date: 2026/02/26
Tang YanJankauskas Stanislovas SLiu LiWang XujunXiaoli Alus MYang FajunSantulli GaetanoFeng DaorongPessin Jeffrey E - Burn-induced sepsis triggers profound intestinal injury, contributing to systemic inflammation and organ damage. Beta-hydroxybutyrate (BHB), a major ketone body, acts as a key regulator of intestinal epithelial regeneration. Its metabolic dysregulation has been implicated in impaired cell proliferation and the maintenance of intestinal stem cells (ISCs). However, the dynamic regulatory mechanisms underlying BHB fluctuation during burn sepsis-induced intestinal injury remain elusive. In this study, we demonstrate that TIGAR expression is markedly reduced in small intestinal crypts of burn sepsis mice. TIGAR deficiency substantially diminishes BHB production and compromises cell proliferation and ISC self-renewal capacity. Mechanistically, the 1-131 domain of TIGAR orchestrate dual functionality: it acts as a mitochondrial targeting signal to direct TIGAR localization and competitively binds the ketogenic enzyme HMGCL, thereby inhibiting its interaction with the E3 ubiquitin ligase Park2. This spatial interference blocks Park2-mediated K48-linked ubiquitination and proteasomal degradation of HMGCL, and stabilizing HMGCL to enhance BHB synthesis. Elevated BHB induces β-hydroxybutyrylation at lysine 335 of β-catenin, which facilitates β-catenin nuclear translocation and strengthens its interaction with TCF4, therefore driving cell proliferation and ISC self-renewal, ultimately maintaining intestinal epithelial regeneration. Collectively, this study identifies a novel role of TIGAR in maintaining intestinal barrier regeneration by promoting ketone body production. This previously unexplored mechanism of TIGAR may serve as a critical compensation for the treatment of burn-related gut barrier dysfunction. - Source: PubMed
Publication date: 2026/02/19
Zhang PanyangWu DanWei YanSu SenZha XuleLiu XiaoyanZhang TingHuang QianyingChen QianBao ZhongweiFan ShijunXia LinPeng Xi