| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Peroxiredoxin 2 |
| Uniprot No | P32119 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-198aa |
| 氨基酸序列 | ASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVC PTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNI PLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRS VDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN |
| 预测分子量 | 22 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. |
1. **"Crystal Structure of Human Peroxiredoxin 2: Structural Insights into Its Catalytic Mechanism"**
*作者：Rhee, S.G. et al.*
摘要：解析了人源PRDX2的晶体结构，揭示了其催化循环中过氧化物底物结合位点及活性位点构象变化，阐明其抗氧化功能的结构基础。
2. **"Recombinant Peroxiredoxin 2 Attenuates Neuronal Apoptosis via ROS Scavenging in Ischemic Stroke Models"**
*作者：Wood, Z.A. et al.*
摘要：研究重组PRDX2蛋白在脑缺血模型中的神经保护作用，证明其通过清除活性氧(ROS)减少神经元凋亡，提示其治疗潜力。
3. **"Peroxiredoxin 2 Suppresses Inflammation by Regulating NF-κB Signaling in Macrophages"**
*作者：Immenschuh, S. et al.*
摘要：发现重组PRDX2通过抑制NF-κB通路减少炎症因子释放，揭示其在调控先天免疫反应中的新功能。
4. **"Biomarker Potential of Recombinant PRDX2 in Cardiovascular Disease Diagnosis"**
*作者：Manevich, Y. et al.*
摘要：评估重组PRDX2作为氧化应激标志物的临床价值，发现其在动脉粥样硬化患者血清中表达异常，与疾病进展相关。
(注：以上为模拟文献示例，实际引用需以真实发表论文为准。)
Peroxiredoxin 2 (PRDX2) is a member of the peroxiredoxin family, a class of highly conserved antioxidant enzymes crucial for maintaining cellular redox homeostasis. It plays a pivotal role in protecting cells from oxidative damage by catalyzing the reduction of reactive oxygen species (ROS), such as hydrogen peroxide (H₂O₂), peroxynitrite, and organic hydroperoxides. PRDX2 is ubiquitously expressed across tissues, with high abundance in erythrocytes, where it safeguards hemoglobin and cell membranes from oxidation. Structurally, it contains a conserved catalytic cysteine residue that undergoes cyclic oxidation and reduction during its enzymatic activity, relying on thioredoxin, thioredoxin reductase, and NADPH for regeneration.
Recombinant PRDX2 protein is produced using expression systems like *E. coli* or mammalian cells, enabling large-scale purification for research and therapeutic applications. Its recombinant form retains native enzymatic activity and stability, making it a valuable tool for studying oxidative stress-related mechanisms in diseases such as neurodegenerative disorders, cancer, diabetes, and cardiovascular conditions. Additionally, PRDX2 has been implicated in cell signaling, inflammation regulation, and apoptosis, extending its biological relevance beyond antioxidant defense.
Research on recombinant PRDX2 also explores its potential as a therapeutic agent or biomarker. For instance, its overexpression has been linked to chemoresistance in cancers, while deficiencies correlate with accelerated aging and neurodegeneration. Post-translational modifications, such as hyperoxidation or phosphorylation, further regulate its function, adding complexity to its role in redox signaling. Overall, recombinant PRDX2 serves as a critical reagent for dissecting oxidative stress pathways and developing targeted interventions for redox-related pathologies.
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