Prdx1
- Known as:
- Prdx1
- Catalog number:
- 031964A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Prdx1
Related genes to: Prdx1
- Gene:
- PRDX1 NIH gene
- Name:
- peroxiredoxin 1
- Previous symbol:
- PAGA
- Synonyms:
- NKEFA
- Chromosome:
- 1p34.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-01
- Date modifiied:
- 2014-11-19
Related products to: Prdx1
anti-PRDX1 / Peroxiredoxin 1 (Internal)Anti-PRDX1 AntibodyAnti-PRDX1 AntibodyAnti-PRDX1, Goat Polyclonal to PRDX1, Isotype , Host GoatAntibodies: PRDX1 HOST: Goat Clonality: pAbAntibody to Peroxiredoxin 1 (PRDX1) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntibody to Peroxiredoxin 1 (PRDX1) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntigens PRDX1, 1-199aa, Human, His tagged , Recombinant, E.coliBiotin-linked Antibody to Peroxiredoxin 1 (PRDX1); Reactivity: Homo sapiens (Human) Clonality: Polyclonal Source: RabbitBos taurus,Bovine,Peroxiredoxin-1,PRDX1Bovine peroxiredoxin 1 (PRDX1) ELISA kit, Species Bovine, Sample Type serum, plasmaBovine Peroxiredoxin-1(PRDX1) ELISA kitBovine Peroxiredoxin-1(PRDX1) ELISA kit SpeciesBovineChicken peroxiredoxin 1 (PRDX1) ELISA kit, Species Chicken, Sample Type serum, plasmaChicken Peroxiredoxin-1(PRDX1) ELISA kit Related articles to: Prdx1
- Hydrogen peroxide (HO) plays a dual role as both a signalling molecule and a mediator of oxidative stress. Although mitochondria are major producers of HO, the relative contributions of mitochondrial versus cytosolic antioxidant systems to mitochondrial HO homeostasis in intact cells remain poorly defined. Here, we combined compartment-resolved live-cell imaging using HyPer7, inducible mitochondrial HO generation (matrix-targeted d-amino acid oxidase), kinetic modelling, and a targeted CRISPR/Cas9 screen to dissect determinants of mitochondrial HO dynamics in HEK293 cells. Unexpectedly, we found that the cytosolic peroxiredoxin PRDX1 is a dominant regulator of mitochondrial matrix HO levels. Loss of cytosolic PRDXs markedly enhanced matrix Hyper7 signals under both exogenous and mitochondria-intrinsic HO production, exceeding the effects of deleting mitochondrial peroxiredoxins. Modelling and transport experiments indicated a very high permeability of the mitochondrial inner membrane to HO enabling rapid efflux and the establishment of steep concentration gradients. This permits the cytosol to function as a major sink to limit matrix HO accumulation. PRDX1 deficiency sensitized cells to chronic mitochondrial oxidative stress. A targeted CRISPR screen identified the Rab7 GAP TBC1D5, linking mitophagy to cellular survival under these conditions. Consistently, PRDX1/2-deficient cells exhibited elevated mitophagic flux, indicating mitochondrial quality control as a compensatory response. Our study reveals that cytosolic PRDXs critically impact mitochondrial redox homeostasis and provides a systems-level framework for understanding compartmental redox control and stress adaptation. - Source: PubMed
Publication date: 2026/04/30
Jacobs Lianne JhcDoll SebastianTrümbach DietrichVeronese MatteoDi Pietro GiadaYapici Fatma IsilHasberg LidwinaGentzsch PascalGerlich SarahHansen Jensvon Karstedt SilviaRugarli Elena IConrad MarcusSalvador ArmindoRiemer Jan - Renal cell carcinoma (RCC) is a highly heterogeneous malignant tumor, characterized by a globally increasing incidence and mortality rate. Although surgical resection serves as the standard treatment for localized RCC, recurrence and metastasis remain major clinical challenges. Based on patient sample analysis and signaling pathway investigation, the present study identifies peroxiredoxin 1 (PRDX1) as a potential therapeutic target for RCC. - Source: PubMed
Publication date: 2026/04/17
Liang ZhiLin XiaochunZeng ShenWu LiliDong YujunZhang ChenLi MeiZhu FudiChen LuNi Suiqin - - Source: PubMed
Publication date: 2026/04/29
Liu XiaohuiZeng LiyiLiu JingHuang YulunYao HuaZhong JinmanTan JiewenGao XuejuanXiong DanLiu Langxia - Dark muscle in fish exhibits distinct nutritional, oxidative, and functional characteristics compared to ordinary muscle. This study aimed to elucidate the underlying biochemical variations of oxidative microenvironment in dark and ordinary muscles in snakehead fish (Channa argus) through multi-omics analyses. Dark muscle exhibited a stronger oxidative signature (higher TBARS and protein carbonyls, lower sulfhydryl content), and higher emulsifying activity/stability but lower buffering capacity, reduced foaming capacity and weaker gelation. Dark muscle contained higher levels of crude fat, protein, iron and glutathione, but lower moisture content and pH. Lipidomics revealed enrichment of mitochondria-associated lipid features, particularly cardiolipin and phosphatidylglycerol, together with glycolipids and highly unsaturated triglycerides; proteomics indicated higher abundance of proteins involved in oxidative phosphorylation, fatty-acid β-oxidation and redox/antioxidant defense (e.g., PRDX1, SOD2, MGST3); and metabolomics showed elevated PUFA-derived oxidation products, TCA-cycle intermediates and redox-related cofactors. By integrating lipidomic, proteomic, and metabolomic data, this study captures concordant changes in lipid composition, oxidative metabolism, and redox-related metabolites, thereby providing a more comprehensive explanation for the techno-functional between dark and ordinary muscles and showing that the oxidation-prone biochemical background of dark muscle is associated with enhanced emulsifying properties but reduced gel-forming ability. - Source: PubMed
Publication date: 2026/04/20
Yu QingqingBao YulongZhang LongtengHong HuiGao Ruichang - - Source: PubMed
Publication date: 2026/04/19
Škopková MartinaKabelíková PavlínaAndrésová AndreaBrennerová KatarínaDallemule SilviaSabo MiroslavPetrovič RóbertGašperíková Daniela