PRDX1 Pre-design Chimera RNAi
- Known as:
- PRDX1 Pre-design Chimera RNAi
- Catalog number:
- H00005052-R01
- Product Quantity:
- 20 nmol
- Category:
- -
- Supplier:
- Abno
- Gene target:
- PRDX1 Pre-design Chimera RNAi
Related genes to: PRDX1 Pre-design Chimera RNAi
- 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 Pre-design Chimera RNAi
Related articles to: PRDX1 Pre-design Chimera RNAi
- 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 - BACKGROUND Primary nonfunction (PNF) is a severe complication following liver transplantation (LT), yet precise molecular biomarkers for early identification of patients at risk remain lacking, which can delay timely therapeutic intervention. MATERIAL AND METHODS Liver biopsies were collected from patients and classified into 4 groups: control, optimal graft (OG), early allograft dysfunction (EAD), and PNF. Samples were obtained at 3 time points: T0 (pre-cold perfusion), T1 (pre-reperfusion), and T2 (post-reperfusion). Isobaric tags for relative and absolute quantitation (iTRAQ) and multiple reaction monitoring (MRM) were used for proteomic analysis and biomarker verification. RESULTS Baseline characteristics of the patients showed no significant differences between groups. A total of 6505 proteins were identified in human liver samples. There were 160 differentially expressed proteins (67 upregulated and 93 downregulated) found in the PNF group compared to the control, while 54 and 36 proteins were identified in the EAD and OG groups, respectively. Ten proteins were selected for MRM verification, confirming the significant upregulation of VWF and downregulation of PRDX1, HGD, THIO, 6PGD, and HPPD, consistent with the iTRAQ results. CONCLUSIONS PRDX1, HGD, THIO, 6PGD, HPPD, and VWF were identified as candidate proteins associated with PNF and ischemia-reperfusion injury (IRI) after LT. These findings are hypothesis-generating and require validation in larger, independent cohorts to determine their potential clinical value. - Source: PubMed
Publication date: 2026/07/14
Lin XiaohongCai WanzhenHong XitaoYe ZimingDong YuqiWang ShuaiHe XiaoshunLi DonghongJu WeiqiangChen Maogen - Bladder cancer represents a significant disease burden in men, as it is both highly common and a leading cause of cancer-related deaths. Despite advances in personalized therapies, patient outcomes continue to show considerable variability, and there is an urgent need to explore novel therapeutic targets for this disease. Ferroptosis has recently been implicated in chemotherapy response and proposed as a therapeutic target in various cancers; however, its regulatory mechanism in bladder cancer cells has not been fully elucidated. In this study, we analyzed public data from the GEO database and found that the transcription factor GLI2 was significantly upregulated in bladder cancer compared with normal bladder tissues. Functional assays revealed that GLI2 promotes malignant progression and represses ferroptosis in bladder cancer cells. Mechanistically, RNA sequencing and chromatin immunoprecipitation (ChIP) assays showed that GLI2 transcriptionally regulates the expression of peroxiredoxin 1 (PRDX1), a well-characterized ferroptosis-inhibiting gene. Additionally, rescue assay results indicated that PRDX1 mediates the role of GLI2 in ferroptosis repression and promotes malignant progression of bladder cancer. More importantly, inhibition of GLI2 via siRNA or a small-molecule inhibitor sensitized bladder cancer cells to both PRDX1 inhibitors and cisplatin. Together, these findings delineate a regulatory axis involving GLI2-PRDX1-mediated ferroptosis, provide mechanistic insights into its critical role in driving bladder cancer progression and chemosensitivity, and offer potential therapeutic targets for future clinical intervention. - Source: PubMed
Publication date: 2026/07/11
Yao YuyangYang PangNiu ShaoruiYang JunTang XiaofengBai WeiChen KangmingZhou YuntongYang XiaorongLv Xiao-Bin