| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | petE |
| Uniprot No | P50057 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-131aa |
| 氨基酸序列 | ATVQIKMGTDKYAPLYEPKALSISAGDTVEFVMNKVGPHNVIFDKVPAGESAPALSNTKLAIAPGSFYSVTLGTPGTYSFYCTPHRGAGMVGTITVE |
| 预测分子量 | 26.2 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petE(质体蓝素)重组蛋白的3篇参考文献及其摘要概括：
1. **《Heterologous expression and characterization of recombinant plastocyanin from Arabidopsis thaliana in E. coli》**
- **作者**: Smith, J.R., & Johnson, L.M.
- **摘要**: 研究通过在大肠杆菌中异源表达拟南芥petE基因，优化表达条件并纯化重组质体蓝素，验证其与天然蛋白相似的铜结合活性和电子传递功能。
2. **《Functional analysis of recombinant plastocyanin from Synechocystis sp. PCC 6803: Role in photosynthetic electron transport》**
- **作者**: Chen, H., & Wang, Y.
- **摘要**: 利用重组petE蛋白在蓝藻中探究质体蓝素在光合作用中的调控机制，发现其缺失导致光系统I电子传递效率显著下降，重组蛋白可恢复表型。
3. **《Crystallographic study of recombinant petE plastocyanin: Insights into metal-binding and redox properties》**
- **作者**: Martínez, A., et al.
- **摘要**: 通过X射线晶体学解析重组质体蓝素的三维结构，揭示其铜离子配位模式及氧化还原电位特性，为人工设计电子传递蛋白提供参考。
注：上述文献信息为示例性质，实际引用需根据具体研究检索真实数据库(如PubMed、Web of Science)。
**Background of petE Recombinant Protein**
The *petE* gene encodes plastocyanin, a small, water-soluble copper-containing protein that plays a critical role in photosynthetic electron transport. Found in plants, algae, and cyanobacteria, plastocyanin functions as a mobile electron carrier, shuttling electrons between cytochrome *b₆f* and photosystem I (PSI) during the light-dependent reactions of photosynthesis. Its redox activity is facilitated by a copper ion coordinated within a conserved binding site, which cycles between Cu(I) and Cu(II) oxidation states.
Recombinant petE protein is produced via heterologous expression systems, most commonly in *Escherichia coli*, enabling large-scale production for structural and functional studies. The protein’s simple structure (a β-sandwich fold with a single copper center), stability, and high solubility make it an attractive model for studying metalloprotein assembly, electron transfer mechanisms, and redox dynamics. Additionally, its distinctive spectroscopic properties (e.g., a strong absorbance peak at 597 nm) allow easy monitoring of its redox state.
Research on recombinant petE has expanded its applications beyond photosynthesis. It serves as a scaffold for engineering novel electron transfer pathways in synthetic biology, a tool for investigating metal ion trafficking, and a component in biohybrid systems for solar energy conversion. Studies also explore its potential in bioremediation due to its metal-binding capacity. Furthermore, petE’s role in oxidative stress responses and interactions with other photosynthetic components provides insights into cellular redox regulation.
Overall, petE recombinant protein bridges fundamental research in bioenergetics with biotechnological innovations, underscoring its versatility as a molecular tool in both basic and applied sciences.
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