| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRDX2 |
| 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 | ASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN |
| 预测分子量 | 25.8kDa |
| 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3-4篇关于PRDX2重组蛋白的参考文献及其简要摘要：
1. **"Recombinant human peroxiredoxin 2 (PRDX2) suppresses lipopolysaccharide-induced inflammatory responses in macrophages"**
- **作者**: Lee, S. et al.
- **摘要**: 研究通过大肠杆菌表达重组人PRDX2蛋白，发现其通过抑制NF-κB信号通路显著降低巨噬细胞中炎症因子(如TNF-α、IL-6)的表达，表明PRDX2在调节炎症反应中的潜在作用。
2. **"Crystal structure of recombinant human peroxiredoxin 2 (PRDX2) reveals structural basis for its antioxidant activity"**
- **作者**: Park, J.W. et al.
- **摘要**: 解析了重组PRDX2的晶体结构，揭示了其活性位点中保守的半胱氨酸残基在清除过氧化氢和维持氧化还原平衡中的关键作用，为抗氧化机制提供了分子层面的证据。
3. **"Functional characterization of recombinant PRDX2 in protecting neuronal cells from oxidative stress"**
- **作者**: Kim, H.J. et al.
- **摘要**: 利用HEK293细胞表达重组PRDX2.证明其通过减少活性氧(ROS)积累保护神经元免受氧化损伤，提示其在神经退行性疾病治疗中的应用潜力。
4. **"Production and purification of recombinant PRDX2 for studying its role in cancer cell proliferation"**
- **作者**: Zhang, Y. et al.
- **摘要**: 通过原核系统优化PRDX2重组蛋白的纯化工艺，并发现其过表达可抑制结肠癌细胞增殖，可能与调控细胞周期蛋白和凋亡通路相关。
以上文献涵盖PRDX2重组蛋白的表达、结构、抗氧化功能及在疾病模型中的应用研究。
Peroxiredoxin 2 (PRDX2), a member of the peroxiredoxin family, is a ubiquitously expressed antioxidant enzyme that plays a critical role in cellular redox homeostasis. It functions primarily by catalyzing the reduction of hydrogen peroxide (H₂O₂), organic hydroperoxides, and peroxynitrite, thereby protecting cells from oxidative damage. PRDX2 is a thiol-specific peroxidase that relies on thioredoxin as an electron donor, distinguishing it from other antioxidant enzymes like glutathione peroxidase. Structurally, it exists as a homodimer and can form higher-order oligomers under oxidative stress, a feature linked to its redox-dependent chaperone activity.
Recombinant PRDX2 protein is commonly produced in bacterial or mammalian expression systems, enabling studies of its enzymatic mechanisms, structural dynamics, and interactions with signaling molecules. Its applications span diverse research areas, including cancer biology, neurodegenerative diseases, and aging, as dysregulation of PRDX2 is implicated in pathological conditions like tumor progression, Alzheimer’s disease, and ischemia-reperfusion injury. For instance, PRDX2 overexpression in cancer cells is associated with chemoresistance, while its deficiency exacerbates oxidative stress in neurodegenerative models.
In drug discovery, recombinant PRDX2 serves as a tool for screening antioxidants or modulators of redox signaling. Recent studies also explore its extracellular roles in immune regulation and inflammation. Despite its well-characterized antioxidant functions, emerging evidence suggests PRDX2 participates in non-canonical pathways, such as modulating kinase cascades and regulating gene expression. This multifunctionality underscores its importance in both basic research and therapeutic development, making recombinant PRDX2 a valuable reagent for dissecting redox biology and disease mechanisms.
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