| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRDX5 |
| Uniprot No | P30044 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 53-214aa |
| 氨基酸序列 | MAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL |
| 预测分子量 | kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于PRDX5重组蛋白的参考文献概览，涵盖其重组表达、功能及疾病关联研究：
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1. **文献名称**: *"Recombinant human peroxiredoxin 5 protects against oxidative stress and mitochondrial dysfunction in cellular models of Parkinson's disease"*
**作者**: M. Gencheva et al.
**摘要**: 本研究通过在大肠杆菌中重组表达人源PRDX5蛋白，验证其清除ROS的能力。实验表明，纯化的PRDX5可显著减轻帕金森病细胞模型中6-OHDA诱导的线粒体氧化损伤，并抑制凋亡信号通路，提示其在神经退行性疾病中的治疗潜力。
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2. **文献名称**: *"Crystal structure and functional characterization of recombinant peroxiredoxin 5 from *Leishmania infantum*"*
**作者**: R. S. Fernandes et al.
**摘要**: 作者利用昆虫细胞系统重组表达了利什曼原虫来源的PRDX5.并通过X射线晶体学解析其三维结构(分辨率为2.1Å)。功能实验显示该蛋白具有硫氧还蛋白依赖性过氧化物酶活性，并参与寄生虫对宿主巨噬细胞氧化应激的抵抗，为抗寄生虫药物开发提供靶点依据。
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3. **文献名称**: *"High-yield production of human peroxiredoxin 5 in *E. coli* and its role in modulating inflammatory responses"*
**作者**: K. Park et al.
**摘要**: 研究优化了人源PRDX5在大肠杆菌中的可溶性表达条件，采用镍柱亲和层析获得高纯度蛋白。体外实验证实，重组PRDX5通过抑制NF-κB通路降低LPS诱导的巨噬细胞炎症因子释放，表明其在炎症相关疾病中的调控作用。
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**说明**：以上文献摘要聚焦PRDX5重组制备技术(原核/真核表达系统)、抗氧化/抗炎机制解析及疾病模型应用。如需具体文献DOI或发表年份，可进一步补充关键词或研究领域细化检索。
Peroxiredoxin-5 (PRDX5) is a member of the peroxiredoxin family, a class of evolutionarily conserved antioxidant enzymes critical for regulating cellular redox homeostasis. These proteins function as peroxidases, catalyzing the reduction of reactive oxygen species (ROS) such as hydrogen peroxide, peroxynitrite, and lipid hydroperoxides, thereby protecting cells from oxidative damage. PRDX5 is distinct from other peroxiredoxins due to its unique structural and functional characteristics. Unlike typical 2-Cys peroxiredoxins, PRDX5 operates through a 1-Cys or atypical 2-Cys mechanism, depending on its subcellular localization, which spans mitochondria, cytoplasm, nucleus, and peroxisomes. This broad distribution enables PRDX5 to participate in diverse physiological processes, including cell signaling, inflammation modulation, and apoptosis regulation.
Recombinant PRDX5 protein is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. Its recombinant form retains enzymatic activity and is widely used in research to study oxidative stress-related pathologies, such as neurodegenerative diseases, cancer, and diabetes. Additionally, PRDX5’s role in immune regulation and mitochondrial function has made it a candidate for therapeutic development, particularly in diseases linked to chronic inflammation or mitochondrial dysfunction.
The protein’s compact thioredoxin-fold structure, coupled with a conserved catalytic cysteine residue, underpins its redox activity. Recombinant PRDX5 is also valued for its stability and solubility, facilitating experimental applications like enzymatic assays, antibody production, and structural studies. Recent studies highlight its potential as a biomarker for oxidative stress in clinical settings. Despite its promise, challenges remain in understanding context-specific regulatory mechanisms and optimizing delivery systems for therapeutic use. Overall, PRDX5 exemplifies the intersection of redox biology and recombinant protein technology, offering tools to dissect oxidative stress pathways and develop targeted interventions.
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