PRDX1 polyclonal antibody
- Known as:
- PRDX1 pab (anti-)
- Catalog number:
- PAB1218
- Product Quantity:
- 100 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- PRDX1 polyclonal antibody
Related genes to: PRDX1 polyclonal antibody
- 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 polyclonal antibody
Related articles to: PRDX1 polyclonal antibody
- Post-translational acetylation of cytoplasmic proteins has emerged as a critical regulatory mechanism in neurological disease. Peroxiredoxin 1 (Prdx1), a key antioxidant enzyme, undergoes reversible lysine acetylation that modulates its enzymatic activity. Histone Deacetylase 6 (HDAC6), a predominantly cytoplasmic deacetylase, has been identified as a regulator of Prdx1 acetylation, linking deacetylase activity to redox homeostasis. Accurate detection of Prdx1 deacetylation requires methodological strategies capable of preserving endogenous acetylation states and selectively enriching acetylated protein fractions. This chapter describes a reproducible workflow for assessing HDAC6-mediated Prdx1 deacetylation in cortical tissue which integrates optimized protein extraction under acetylation-preserving conditions, acetyl-lysine-based co-immunoprecipitation, and immunoblot detection of Prdx1. Parallel assessment of total Prdx1 and established HDAC6 substrates enables normalization and validation of deacetylase activity. Quantitative densitometric analysis provides comparative evaluation of acetylation levels across experimental conditions. This methodology offers a practical and translationally applicable approach for investigating non-histone deacetylation mechanisms and can be adapted to other HDAC6-regulated substrates in neurodegenerative research. - Source: PubMed
Publication date: 2026/06/17
Kumar SonaliShanker Ozasvi RBanerjee JyotirmoyDixit Aparna Banerjee - Reactive oxygen species (ROS) promote genomic instability and fuel oncogenic signaling in cancer, but antioxidant therapies have so far failed to improve, or worsen, cancer outcomes. Emerging data suggest that T cells depend on ROS for signal transduction. In this study, we show that tumors exploit this dependency, releasing antioxidant enzymes into the tumor environment to suppress T cell-mediated antitumor immunity. The interstitial fluid of tumors possesses potent antioxidant activity, associated with enrichment of the antioxidant enzyme peroxiredoxin 1 (PRDX1). Extracellular PRDX1 deprives T cells of ROS, preventing oxidative inactivation of phosphatases required for T cell receptor-driven kinase signaling and effector function. is up-regulated upon cancer immunoediting, and loss of PRDX1 within tumors enhances antitumor immunity and immunotherapy responses. These findings define a redox-dependent mechanism of tumor immunosuppression that is potentially amenable to therapeutic intervention. - Source: PubMed
Publication date: 2026/09/03
Wesolowski Alexander JPillay Ardon MVardaka PanagiotaNasrallah RababGreaves RandyLi HousaiyinLoffreda IlianaJenkin ChelseaJames Andrew MNübling AlicaWard Christopher Jvon Linde TeresaConti Alberto GTzeng Sheue-FenDahmani LaylaEvans Alexander CWhiteside Sarah KYamashita-Kanemaru YumiImianowski Charlotte JYang JieGonzalez Ignacio MoragaChapman JackAl-Deka AwsOkkenhaug KlausMurphy Michael PSwiatczak BartlomiejGuittard GeoffreyLugli EnricoFlatz LukasHo Ping-ChihEil Robert LRoychoudhuri Rahul - Hyperactivation of Wnt/β-catenin signaling drives colorectal cancer (CRC) progression and contributes to an immunosuppressive tumor microenvironment. Although peroxiredoxin-1 (PRDX1) is overexpressed in CRC and correlated with poor prognosis, its mechanistic role in Wnt/β-catenin-mediated immune evasion remains unclear. Through transcriptomic sequencing and co-immunoprecipitation, we identified PRDX1-interacting proteins and validated their functional roles via luciferase assays, mutagenesis, and pharmacological approaches in syngeneic models. Results demonstrated that PRDX1 knockout attenuated Wnt/β-catenin signaling in AOM/DSS-induced CRC mice. In cellular models, PRDX1 knockdown inhibited nuclear translocation of β-catenin by promoting its ubiquitination. Mechanistically, PRDX1 functions as a redox-sensitive chaperone that interacts with protein arginine methyltransferase 5 (PRMT5) in the cytoplasm and facilitates its nuclear translocation. This was associated with increased H3R2me2 and H3R8me2 levels, upregulation of DVL3 transcription, and subsequent Wnt/β-catenin activation. The interaction was abrogated by disrupting the Rossmann-fold or β-barrel domains of PRMT5, or by introducing the R368A catalytic mutation, suggesting that these domains are important for the PRDX1-PRMT5 association. Importantly, pharmacologically inhibiting PRMT5 suppressed PRDX1-driven tumor growth and alleviated immunosuppression in vivo by dampening Wnt/β-catenin signaling. These findings identify a novel PRDX1-PRMT5 axis that activates Wnt/β-catenin signaling, highlighting a potential therapeutic strategy for CRC by targeting this pathway to suppress tumor progression and remodel the immune microenvironment. - Source: PubMed
Publication date: 2026/08/27
Yu NianhuaLi XiHan JinliWang XiaohuiZeng ChenghongSun YuqiTie JingyanXu XiangyiQu XianjunYu Xinfeng - Osteoclastogenesis is driven by tightly coordinated transcriptional programs downstream of receptor activator of nuclear factor-κB ligand (RANKL) signaling, in which reactive oxygen species (ROS) function as essential secondary messengers. Although extracellular peroxiredoxin 1 (PRDX1) has been implicated in the suppression of osteoclast differentiation, the role of intracellular PRDX1 in regulating osteoclastogenic signaling remains poorly understood. Here, we identify intracellular PRDX1 as a redox-sensitive negative regulator of osteoclastogenesis and bone resorption. PRDX1 deficiency markedly enhanced osteoclast differentiation, bone resorption activity, and osteoporotic phenotypes in vivo. Transcriptomic and mechanistic analyses revealed that PRDX1 attenuates osteoclastogenic gene transcription by blocking the nuclear factor kappa B (NF-κB)/p65 signaling axis. Loss of PRDX1 increased intracellular ROS accumulation, promoted p65 nuclear translocation and promoter occupancy, thereby amplifying osteoclastogenic transcriptional programs. Mechanistically, PRDX1 underwent TNF receptor associated factor 6 (TRAF6)-mediated Lys67-dependent ubiquitylation and lysosomal degradation in response to RANKL signaling. In addition, RANKL-induced Src activation promoted phosphorylation of PRDX1 at Tyr194, which enhanced TRAF6-mediated ubiquitylation without substantially altering overall TRAF6 binding. Together, these findings reveal a PRDX1-ROS feedback loop that modulates NF-κB activity during osteoclastogenesis and identify regulated PRDX1 degradation as a mechanism by which RANKL signaling amplifies osteoclastogenic responses. These findings establish intracellular PRDX1 as an important modulator of skeletal homeostasis, suggesting its potential relevance as a pharmacological target in diseases characterized by excessive bone resorption. - Source: PubMed
Publication date: 2026/08/27
Lee HyerimLee SheunghunJang You-JeeLee KyubinHwang Seon YoungOh Goo TaegPark Jae-IlYi Sun-JuKim Kyunghwan - Preeclampsia (PE) affects 2-8% of pregnancies and causes > 76,000 maternal deaths annually. The mechanistic link between placental oxidative stress and angiogenic failure remains poorly defined, and no validated multi-gene biomarker panel exists for early detection. In particular, how antioxidant enzymes such as PRDX2 interact with angiogenic regulators (VEGFA, ENG) to drive network rewiring in the PE placenta has not been characterized across independent cohorts. This study aimed to characterize the transcriptomic interdependencies between oxidative stress defense, cytokine signaling, and angiogenic regulation across five independent PE placental GEO cohorts. - Source: PubMed
Publication date: 2026/08/10
Kong XiaojuanLiu PengQiao JiangTan ZenyuLei Lei