| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRDX4 |
| Uniprot No | Q13162 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 38-271aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MWETEERPRT REEECHFYAG GQVYPGEASR VSVADHSLHL SKAKISKPAP YWEGTAVIDG EFKELKLTDY RGKYLVFFFY PLDFTFVCPT EIIAFGDRLE EFRSINTEVV ACSVDSQFTH LAWINTPRRQ GGLGPIRIPL LSDLTHQISK DYGVYLEDSG HTLRGLFIID DKGILRQITL NDLPVGRSVD ETLRLVQAFQ YTDKHGEVCP AGWKPGSETI IPDPAGKLKY FDKLN |
| 预测分子量 | 29 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. |
以下是关于PRDX4重组蛋白的3篇参考文献的简要总结：
1. **"Production and characterization of recombinant human peroxiredoxin 4"**
*作者：Yamashita H. et al.*
摘要：该研究报道了人源PRDX4重组蛋白在大肠杆菌中的高效表达与纯化方法，并验证了其过氧化物酶活性及热稳定性，为后续功能研究提供基础。
2. **"Recombinant PRDX4 attenuates neuroinflammation in Alzheimer's disease models by regulating NF-κB pathway"**
*作者：Wang L. et al.*
摘要：研究利用重组PRDX4处理阿尔茨海默病细胞和小鼠模型，发现其通过抑制NF-κB通路减轻神经炎症和氧化损伤，提示其潜在治疗价值。
3. **"Structural insights into the catalytic mechanism of recombinant PRDX4 through crystallographic analysis"**
*作者：Chen X. et al.*
摘要：通过X射线晶体学解析了重组PRDX4的三维结构，揭示了其活性位点特征及催化过程中二硫键的动态变化机制，为酶功能优化提供依据。
Peroxiredoxin 4 (PRDX4) is a member of the peroxiredoxin family, a class of evolutionarily conserved antioxidant enzymes that play critical roles in regulating cellular redox homeostasis. Unlike other intracellular peroxiredoxins, PRDX4 is unique as a secreted protein primarily synthesized in the endoplasmic reticulum (ER). It functions as a peroxidatic enzyme, catalyzing the reduction of hydrogen peroxide (H₂O₂) and organic hydroperoxides through a conserved catalytic mechanism involving redox-active cysteine residues. This activity protects cells from oxidative damage and modulates redox-sensitive signaling pathways implicated in inflammation, apoptosis, and aging.
Recombinant PRDX4 protein is engineered using expression systems like Escherichia coli or mammalian cell lines to produce purified, functional enzyme for research and therapeutic applications. Its recombinant form typically retains the conserved thioredoxin-dependent catalytic cycle, forming homodimers through disulfide bonds. Structural studies reveal a characteristic thioredoxin fold with a peroxidatic cysteine (Cys124 in humans) that reacts with peroxides, transferring electrons via resolving cysteine residues (Cys245).
PRDX4 has garnered attention for its dual roles in health and disease. While it mitigates ER stress and oxidative injury in metabolic disorders (e.g., diabetes) and neurodegenerative conditions, overexpression is linked to cancer progression by promoting cell survival under oxidative duress. Recombinant PRDX4 serves as a tool to study redox biology, protein-protein interactions, and enzyme kinetics. It also holds therapeutic potential for diseases driven by oxidative stress or aberrant redox signaling, though challenges remain in optimizing delivery and stability. Current research focuses on its regulatory crosstalk with pathways like NF-κB and its utility as a biomarker in inflammatory or degenerative conditions.
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