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
- Oral ulcers (OU), as the most highly prevalent and recurrent oral mucosal lesion, have an unclear pathogenesis that hampers the development of effective treatments. While emerging evidence suggests that deubiquitinating enzymes (DUBs) may play a role in oral diseases, their functions in OU remain unclear. In this study, we screened the expression of DUBs in tongue tissues from mice with OU and identified OTU domain-containing protein 6A (OTUD6A) as the most substantially downregulated DUB during OU progression. The functional studies demonstrated that OTUD6A deficiency exacerbated OU pathology in mice and, correspondingly, suppressed proliferation and migration while promoting apoptosis of human oral keratinocytes (HOKs). Mechanistic investigations revealed that OTUD6A directly bound to peroxiredoxin-1 (PRDX1) and cleaved its K48-linked polyubiquitin chains at lysine 136 site (K136) via the catalytic residue C152, thereby stabilizing PRDX1 in HOKs. Loss of OTUD6A led to PRDX1 degradation, which enhanced mitochondrial oxidative stress and dysfunction, ultimately impairing HOKs function, while OTUD6A overexpression rescued HOKs malfunction. Importantly, local administration of recombinant OTUD6A protein significantly accelerated OU healing in mice. Collectively, these results identify a new OTUD6A-PRDX1 axis in OU pathology and present OTUD6A as a promising therapeutic target for OU. - Source: PubMed
Publication date: 2026/08/12
Sun XiaoyuJia RuiweiPan XingbeiHuang RuiChen JiahongYao ZiyiYin LeiMa JunWang HongjieliangHuang XinyuMa YilinPing YifanChen YuanyuanWang HuiningHuang ShengbinLiang Guang - Non-alcoholic fatty liver disease (NAFLD) is a globally prevalent chronic liver disease, and its progression is closely associated with Kupffer cells (KCs). This study aims to characterize C-X-C motif chemokine ligand 9꞉secreted phosphoprotein 1 (CS) polarization in KCs and investigate its intercellular communication with endothelial cells (ECs) in NAFLD. - Source: PubMed
Lu YaoNi WenjuanChen RongcuiWang Wei - Oridonin is a bioactive diterpenoid derived from the widely used traditional Chinese medicinal herb , exhibits broad-spectrum anti-cancer activity, with several derivatives currently in clinical trials. However, the molecular mechanism underlying its anticancer effects, especially its direct target proteins, remain to be fully elucidated. Here, we found that Oridonin promoted intracellular reactive oxygen species (ROS) accumulation, which in turn induced endoplasmic reticulum (ER) stress-mediated apoptosis. Moreover, ER stress was instrumental in inducing autophagy after Oridonin treatment, while blockade of autophagy further exacerbated Oridonin-induced cytotoxicity. Notably, using activity-based protein profiling (ABPP), we identified the anti-oxidant enzyme Peroxiredoxin 1 (PRDX1) as a key direct covalent target of Oridonin. By binding to Cysteine 173 of PRDX1, Oridonin increased intracellular ROS levels. Furthermore, PRDX1 over-expression mitigated, whereas PRDX1 knockdown potentiated, Oridonin-induced ROS accumulation, autophagy, and subsequently apoptosis. Overall, our results indicate that PRDX1 is a direct covalent binding target mediating Oridonin-induced apoptosis. These findings not only provide fresh insights into the core mechanism of Oridonin-induced cytotoxicity, but also highlight PRDX1 as a potential therapeutic target for renal cancer drug development. - Source: PubMed
Publication date: 2026/06/17
Ding ZiyangWang SisiChen JunhuiSong YaliZhu ZhouTong HaiboIyaswamy AshokChen PengWei XuZhang WeiWang JigangYang ChuanbinFeng Yulin - Influenza viruses, characterized by antigenic drift and shift, can cause seasonal epidemics or pandemics. According to World Health Organization (WHO) data, approximately 650,000 global annual deaths are attributed to influenza-associated respiratory diseases, highlighting the urgent need for vaccine protection in high-risk populations. Residual host cell protein (HCP) may elicit allergic reactions or compromise antigen stability, with their permissible limits stringently regulated by international health authorities. This study employed liquid chromatography-tandem mass spectrometry (LC-MS) to systematically evaluate a downstream purification process involving ultrafiltration concentration coupled with Capto™ Core 700 multimodal chromatography and anion-exchange chromatography (AEC). Key results demonstrated that ultrafiltration concentration of the viral harvest significantly reduced HCP content, achieving a removal rate of 90.32%. Subsequent purification steps further eliminated HCP, with gel filtration chromatography and AEC providing removal rates of 92.47% and 61.52%, respectively. Concurrently, the principal antigen hemagglutinin (HA) increased from 2.21% to 8.61% in the viral bulk. HCP residuals were reduced to 535.67 ng per dose, while residual recombinant nuclease fell below the detection limit of 0.312 ng/mL. Proteomic profiling indicated substantial changes in dominant HCP species following ultrafiltration, with Annexin A2 (ANXA2), Actin cytoplasmic 2 (ACTG), and IF rod domain-containing protein predominating in the concentrate. The subsequent purification maintained consistent HCP profiles, primarily composed of ANXA2, ACTG, and Peroxiredoxin-1 (PRDX1). Overall, ultrafiltration critically reduces HCPs and process-related impurities, while multimodal chromatography effectively enriches key antigens (HA/NA). The established LC/MS platform might provide a robust analytical framework for influenza vaccine quality control and process optimization. - Source: PubMed
Publication date: 2026/07/25
Liu BoLi FangYang YingTu HaoHao PengliangMa QuangangLe YangZhang QingmeiLi XuedanQiu RanYu JiejingZhang ZhegangMeng ShengliYang ZhixingYu Longjiang - Ischemic stroke (IS) is a major cause of death and long-term disability worldwide. Multiple complex biological processes contribute to IS-related neuronal death, among which oxidative stress plays a central role in disease progression. Increasing evidence suggests that oxidative stress-induced neuronal injury is closely associated with ferroptosis and mitochondrial dysfunction, both of which contribute to excessive reactive oxygen species accumulation, lipid peroxidation, and impaired cellular energy metabolism during cerebral ischemia. However, their relative contributions and associated molecular signatures in IS have not been systematically compared. Therefore, this study aimed to identify ferroptosis- and mitochondria-associated genes involved in oxidative stress and neuronal injury in IS and to explore their potential as therapeutic targets for ischemic brain injury. - Source: PubMed
Publication date: 2026/07/10
Ma KeJiang YijingYang YihanRao TingZhan YingYin ZihanDan YuqinXu SihanYang Shanli