PRDX1 monoclonal antibody, clone 2A4
- Known as:
- PRDX1 mab (anti-), clonality 2A4
- Catalog number:
- MAB0713
- Product Quantity:
- 100 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- PRDX1 monoclonal antibody clone 2A4
Related genes to: PRDX1 monoclonal antibody, clone 2A4
- 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 monoclonal antibody, clone 2A4
Related articles to: PRDX1 monoclonal antibody, clone 2A4
- Ischemic stroke triggers profound neuroinflammation and autophagic stress, driven predominantly by microglial overactivation. However, effective therapies targeting this pathogenesis remain elusive. Here, we report the use of 3-hydroxydehydroleucodin (3-Hyd), the primary active component from Kudiezi injection used in China for ischemic stroke patients, as a potent neuroprotective agent that markedly reduces the cerebral infarct area and improves neurological deficits in a mouse model of transient middle cerebral artery occlusion (tMCAO). Integrated bulk RNA sequencing and in vitro assays revealed that 3-Hyd significantly suppressed the microglial proinflammatory phenotype and excessive autophagic flux. Mechanistically, through chemical biology approaches, we discovered that 3-Hyd directly binds to the V51 and R128 residues of peroxiredoxin 1 (PRDX1), which physically disrupts the pathological binding of PRDX1 to its E3 ubiquitin ligase TRIM21, thus preventing the polyubiquitination of PRDX1 at the K109 residue and its subsequent proteasome degradation. Consequently, stabilized PRDX1 impedes TRAF6 ubiquitination, effectively blocking the downstream NF-κB signaling cascade. Strikingly, the anti-neuroinflammatory and cerebroprotective effects of 3-Hyd were largely abolished in microglia-specific Prdx1 conditional knockdown (Cx3cr1) mice. Together, our findings elucidate a novel TRIM21-PRDX1-TRAF6 signaling axis that governs microglial homeostasis and highlight the pharmacological stabilization of PRDX1 by 3-Hyd to block the binding of TRIM21 with PRDX1 as a promising therapeutic strategy for ischemic stroke. - Source: PubMed
Publication date: 2026/09/09
Liu KuiWang LingChen ZhuoQiu Yu-XuanGao Jia-HongXie Ting-TingLi YueHuang HeHu YangHu Li-HongPang Tao - Peroxiredoxin 1 (PRDX1) is a highly conserved, thiol-dependent peroxidase that rapidly scavenges reactive oxygen species to modulate redox signaling. PRDX1-null mice exhibited genomic instability, shortened life span, and accelerated tumorigenesis, including development of lymphomas, sarcomas, and carcinomas. Despite extensive characterization of these phenotypes, the molecular mechanism by which PRDX1 loss causes genomic instability remains poorly understood. Here, we show that PRDX1 deficiency alters nucleolar morphology, impairs RNA polymerase I (POL-I)-dependent transcription of pre-ribosomal RNAs, and triggers nucleolar genomic instability. This oxidative stress-induced nucleolar dysfunction promotes the stability of secondary DNA structures, such as RNA-DNA hybrids and G-quadruplex DNA, contributing to nucleolar genomic instability. We demonstrate that PRDX1 loss reduces nascent ribosomal RNA (rRNA) levels and impairs rRNA processing, further affecting ribosome biogenesis. Mechanistically, we established that PRDX1 loss triggers activation of the nucleolar DNA damage response characterized by activation of the DNA repair kinase ATM and elevated TCOF1 within the nucleolus. In addition, we observed recruitment of the MRE11-RAD50-NBS1 (MRN) complex subunit NBS1 to ribosomal DNA (rDNA) loci and this was further increased under oxidative stress. NBS1 accumulation correlates with the repression of rDNA transcription by POL-I, potentially delaying rRNA synthesis, and safeguarding the nucleolar genome from further oxidative damage. Collectively, these findings uncover a previously unrecognized, but critical role, for PRDX1 in maintaining nucleolar integrity and ribosomal biogenesis through redox-dependent regulation of rDNA transcription and processing machinery. - Source: PubMed
Publication date: 2026/09/09
Gujar VaibhaviFurusawa TakashiSharma ShaluBoateng FrimpongLi HaojianAchour CyrinneTaniyama DaikiKruhlak MichaelPommier YvesOberdoerffer ShaliniStracker Travis HWeyemi Urbain - The DNA damage response (DDR) is a sophisticated network of cellular pathways whose perturbation leads to genome instability and is a key hallmark of oncogenesis. Here, we present data from 32 genome-scale loss-of-function CRISPR interference chemical-genetic screens with inhibitors targeting core constituents of the DDR machinery (PARP, ATR, ATM, DNAPK and WEE1), as both single agents and in combination with poly(ADP-ribose) polymerase inhibitors. These experiments identify >1,000 genes whose perturbation modifies the DDR and provides a rich resource to the DDR community. In addition, this compendium of functional genomics data reveals key principles governing the DDR and highlights a strong chemical-genetic interaction between loss of activity of the peroxiredoxin PRDX1 and all tested DDR inhibitors through a mechanism involving iron availability mediated by an MRGBP-PAX7-IREB2 axis. Our data position PRDX1 as a key suppressor of DNA damage accumulation and potential druggable target in combination with DDR inhibitors. - Source: PubMed
Publication date: 2026/09/08
O'Loughlin Thomas AArab AbolfazlMisiukiewicz SaraMontesano ElizabethYogodzinski ChristopherBorah Ashir AQuarantotti ValentinaLou KevinRosen Barry SCorn Jacob EGianni DavideKabir ShaheenForment Josep VGilbert Luke A - Bladder cancer is characterized by redox adaptation and metabolic plasticity, but the mechanisms linking these processes remain incompletely understood. Integrating bulk, single-cell, and spatial transcriptomic analyses, we identified PRDX1 as a malignant epithelial cell-associated factor linked to adverse outcome. Genetic gain- and loss-of-function studies showed that PRDX1 promoted proliferation, motility, and xenograft growth while limiting reactive oxygen species accumulation and mitochondrial apoptosis. Proteomic and biochemical analyses identified an association between PRDX1 and SCD1. PRDX1 prolonged the SCD1 protein half-life without detectably altering SCD1 transcript abundance and increased USP7-SCD1 co-precipitation. USP7 removed K48-linked polyubiquitin chains from SCD1 and prevented its proteasomal degradation, whereas catalytically inactive USP7 failed to deubiquitinate SCD1. Deletion of PRDX1 residues 157-199 weakened its association with SCD1 and reduced USP7-SCD1 co-precipitation. Depletion of SCD1 or USP7 suppressed PRDX1-dependent growth in vitro and in xenografts. These findings support a model in which PRDX1 facilitates USP7-dependent stabilization of SCD1 and promotes bladder cancer progression. - Source: PubMed
Publication date: 2026/09/07
Wang LiYang JianweiWan ShunLi KunpengJiao PanpanDeng YidiLiu HanlinChen SiyuSi XiaoqiangYang Li - Moyamoya disease, a rare chronic cerebrovascular disorder, requires invasive digital subtraction angiography (DSA) for diagnosis. This study employed high-throughput proteomics to identify plasma biomarkers for Moyamoya disease diagnosis. We conducted immunopanel analysis using the Olink platform to evaluate 92 immune-related proteins in plasma samples from 88 Moyamoya disease patients and 88 healthy controls. Key proteins were identified through differential expression analysis, GO, and KEGG enrichment analysis. A diagnostic model was constructed using LASSO regression, Boruta algorithm, and machine learning models including random forest and XGBoost. Validation of these proteins was performed using GEO external data sets, followed by prediction of potential therapeutic drugs and molecular docking validation through pharmacogenomic databases. A total of 44 differentially expressed proteins were identified through the Olink immunopanel, with 12 downregulated and 32 upregulated. GO and KEGG analyses revealed significant enrichment of these proteins in innate immune responses and signaling pathways such as NF-kB and MAPK. Through LASSO, random forest, and protein under-area analysis, four potential biomarkers for Moyamoya disease (MGMT, SIT1, PRDX1, TRAF2) were identified. A diagnostic model using these proteins showed the highest AUC value with the XGBoost model. Additionally, TRAF2 and PRDX1 exhibited significant expression differences in Moyamoya disease patients within the GEO data set. Our study revealed the immune landscape of Moyamoya disease, identified four biomarkers, and established a variety of diagnostic models. - Source: PubMed
Zhang ZhimengXu HaitaoHou ZiyiNi HaojinLi YongZhou ShengjunWei JieHan LiyuanZhang JunjunDai ZifengXiao YouchaoLin JinghuiGao Xiang