PRDX2_RAT Prdx2 ELISA tesk kit
- Known as:
- PRDX2_RAT Prdx2 Enzyme-linked immunosorbent assay test tesk reagent
- Catalog number:
- gen15081
- Product Quantity:
- 1
- Category:
- Peptides
- Supplier:
- Other suppliers
- Gene target:
- PRDX2_RAT Prdx2 ELISA tesk kit
Related genes to: PRDX2_RAT Prdx2 ELISA tesk kit
- Gene:
- PRDX2 NIH gene
- Name:
- peroxiredoxin 2
- Previous symbol:
- TDPX1
- Synonyms:
- PRP, NKEFB, TSA, PRXII, PRX2, MGC4104
- Chromosome:
- 19p13.13
- Locus Type:
- gene with protein product
- Date approved:
- 1995-07-06
- Date modifiied:
- 2016-10-05
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- Radon exposure is the second most important risk factor for lung cancer after tobacco smoking and represents a significant but often underestimated public health problem. Due to the absence of specific clinical manifestations at early stages, the identification of molecular biomarkers reflecting early radon-induced carcinogenic processes is of particular importance. The aim of this study was to identify protein biomarkers associated with radon exposure in lung cancer patients residing in settlements of the Akmola and North Kazakhstan regions of Kazakhstan. Indoor radon exposure was assessed using CR-39 detectors to measure radon concentrations in residential dwellings during summer and autumn periods. The study included 57 lung cancer patients and 73 control subjects residing in areas characterized by varying levels of radon exposure. Plasma samples were collected and analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS) to identify differentially expressed proteins associated with lung cancer and radon exposure. Statistical analyses were performed to evaluate differences between groups and associations between radon exposure and molecular biomarkers. Seasonal variability in indoor radon concentrations was observed, with several settlements demonstrating levels exceeding international reference values. Proteomic analysis identified multiple proteins differentially expressed between lung cancer patients and controls, as well as between radon-exposed and non-exposed lung cancer patients. Several proteins involved in inflammation, lipid metabolism, oxidative stress, and immune regulation pathways demonstrated significant differences in expression levels, suggesting potential associations with radon-induced carcinogenic mechanisms. LC-MS/MS proteomic profiling identified multiple differentially expressed proteins associated with lung cancer and radon exposure after false discovery rate correction. Proteins involved in inflammation, oxidative stress, immune regulation, and lipid metabolism, including ORM2, AZGP1, PRDX2, IRF7, and APOC3, demonstrated significant expression differences between radon-exposed and low-exposure groups. The identified protein biomarkers demonstrated significant associations with both radon exposure and lung cancer status, indicating their potential relevance for early detection and risk assessment of radon-induced lung cancer. The integration of environmental exposure assessment with proteomic profiling may provide new insights into the molecular mechanisms of radon-associated carcinogenesis and support the development of preventive strategies. - Source: PubMed
Publication date: 2026/05/27
Kazhiyakhmetova BaglanAltaeva NursuluBakhtin MeiratTarlykov PavelOmori YasutakaTokonami ShinjiKranrod ChutimaPradana RadhiaMusikawan SaowarakLesbek AnelIbrayeva DanaraSaifulina ElenaAuganova DanaAumalikova MoldirKairullova MadinaShokabayeva AigerimBizhanova DinaraKashkinbayev Yerlan - The incidence of esophageal adenocarcinoma (EAC) is rapidly increasing in Western countries. Gastroesophageal reflux, containing acidic bile salts (ABS), is the main risk factor for EAC. Cancer cells develop adaptive abilities to recalibrate redox balance via hijacking the antioxidant systems to maintain reactive oxygen species (ROS) below lethal levels. We investigated the role of PRDX2 and its regulation in EAC chemoresistance under reflux conditions. - Source: PubMed
Publication date: 2026/06/09
Chen LeiBallout FarahChen ZhengThangaretnam KrishnapriyaQue JianwenChen Xi StevenMcDonald Oliver GeneZaika AlexanderLivingstone AlanGiordano SilviaShiekhattar RaminLu HengPeng DunfaEl-Rifai Wael - Adipose tissue-derived extracellular vesicles (adiposomes) carry a protein cargo that we previously showed differs between obese and lean individuals. In this study, we investigate how adiposomal protein cargo changes in response to sleeve gastrectomy and examine whether these changes are associated with clinical improvements. Twenty-three obese adults underwent pre- and post-bariatric surgery adipose sampling for adiposome isolation and clinical assessments that included vascular and metabolic profiles and inflammatory markers. The adiposomal protein cargo was analyzed via non-targeted proteomics. Differential protein abundance, pathway enrichment, and correlation analyses were assessed. Twelve weeks after bariatric surgery, BMI and fat mass decreased, accompanied by improved glucose and lipid profiles. Inflammatory markers (leptin, IL-6, CRP) also declined, while adiponectin and nitric oxide increased. Adiposomal proteomics identified 287 proteins, with 138 significantly altered. Downregulated proteins included PRDX2, FN1, SERPIND1, and inflammatory mediators; upregulated proteins included talin-1, fibrinogens, and adiponectin. Correlation analysis linked these changes to improvements in lipid profiles, vascular function, and circulating inflammatory markers. Pathway analysis revealed inhibition of lipid-regulatory pathways alongside enrichment of immune, metabolic, and vascular pathways, including lipoprotein metabolism and endothelial signaling. Bariatric surgery-induced cardiometabolic improvements were accompanied by adiposome proteomic remodeling, characterized by reduced inflammation and metabolic reprogramming. - Source: PubMed
Publication date: 2026/05/29
Asada Monica CRakab Mohamed SaadMirza ImaduddinScichilone GiorgiaMorsy Mohammed HMostafa AmroBianco Francesco MAli Mohamed MHassan ChandraMasrur Mario AMahmoud Abeer M - Fasting induces conserved metabolic and redox adaptations that promote stress resistance and longevity. However, the molecular mechanisms linking transient redox changes and altered metabolism to downstream signalling events remain incompletely understood. Using Caenorhabditis elegans, the roles of peroxiredoxins in coordinating redox-dependent responses to fasting and refeeding were determined. A 4-hr fasting protocol over 5 days extended lifespan, improved late-life physiological activity, reduced age-related lipofuscin and lipid accumulation. The fasting protocol generated a transient increase in mitochondrial ROS, promoted mitochondrial turnover, and attenuated age-related mitochondrial fragmentation. These adaptive responses required the activation and nuclear localisation of the stress-responsive transcription factors DAF-16/FOXO and SKN-1/Nrf2. However, these adaptive responses were abolished in prdx-2 and prdx-6 mutant strains, which exhibited persistent redox imbalance, mitochondrial fragmentation, altered stress resistance, and disrupted DAF-16 and SKN-1 signalling. Mechanistically, loss of 2-Cys PRDX-2 impaired activation of the p38 MAPK PMK-1 pathway, resulting in defective SKN-1 activation. In contrast, loss of 1-Cys PRDX-6 disrupted lipid metabolic signalling, preventing induction of NHR-80 and downstream fatty acid desaturases required for metabolic adaptations. Despite distinct initial signalling pathways, both peroxiredoxins converged on the regulation of DAF-16 and SKN-1. Together, these findings identify PRDX-2 and PRDX-6 as redox sensors that translate a fasting-induced transient ROS signature into mitochondrial and lipid remodelling pathways to promote healthy ageing. - Source: PubMed
Publication date: 2026/05/22
Li PenglinZheng YatingCasas-Martinez Jose CXia QinMiranda-Vizuete AntonioGoljanek-Whysall KatarzynaMcDonagh Brian - To investigate how loganetin, an active compound from Cornus officinalis, inhibits acute myeloid leukemia (AML) by regulating CDK2 ubiquitination-mediated degradation. - Source: PubMed
Ding Ji-YuanZheng WeiZhang Yu-MeiMa Chen-ChenYue Long-TaoLiu KuiWang Zhen-ZhenWang Lin-QiaoMeng XuanWang Jing-Yi