| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tdnL |
| Uniprot No | Q93JW0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-63aa |
| 氨基酸序列 | MPFAQIYMIEGRTEAQKKAVIEKVSQALVEATGAPMANVRVWIQEVPKENWGIAGVSAKELGR |
| 预测分子量 | 6,9 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tdnL重组蛋白的假设性参考文献(基于领域知识推测，非真实文献)：
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1. **文献名称**: *Cloning and Expression of tdnL Gene Encoding a Novel Toluene Dioxygenase in Pseudomonas*
**作者**: Yamamoto H., et al.
**摘要**: 本研究报道了从Pseudomonas putida中克隆tdnL基因，并在大肠杆菌中成功表达重组蛋白。该蛋白具有甲苯双加氧酶活性，催化芳香烃底物的羟基化反应，为生物降解工程提供新工具。
2. **文献名称**: *Structural Characterization of Recombinant TdnL Protein by X-ray Crystallography*
**作者**: Smith J., Patel R.
**摘要**: 通过X射线晶体学解析了tdnL重组蛋白的三维结构，揭示了其活性位点的铁硫簇结合模式及底物识别机制，为酶理性改造奠定结构基础。
3. **文献名称**: *Application of TdnL Recombinant Protein in Industrial Biocatalysis*
**作者**: Li W., et al.
**摘要**: 探讨tdnL重组蛋白在合成手性药物中间体中的应用，证明其高效催化苯衍生物不对称氧化能力，显著提升产物对映体过量值(ee值)。
4. **文献名称**: *Functional Analysis of TdnL in Microbial Degradation Pathways*
**作者**: García-Sánchez M., et al.
**摘要**: 通过基因敲除实验证实tdnL在甲苯代谢途径中的关键作用，重组蛋白的酶动力学分析显示其对多种多环芳烃具有广谱底物适应性。
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注：以上文献为模拟示例，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of TdnL Recombinant Protein**
The TdnL recombinant protein is a engineered variant derived from the *tdnL* gene, which is part of bacterial operons involved in toluene or related aromatic hydrocarbon metabolism. Initially identified in *Pseudomonas* species, the *tdnL* gene encodes a dioxygenase enzyme critical for degrading toluene derivatives into less toxic intermediates, a process essential for environmental bioremediation. The recombinant TdnL protein is produced via heterologous expression systems, typically *Escherichia coli*, using plasmid vectors that enable high-yield protein synthesis under controlled conditions.
Structurally, TdnL belongs to the Rieske non-heme iron dioxygenase family, characterized by conserved iron-binding motifs and a Rieske [2Fe-2S] cluster, which facilitate its catalytic role in oxidizing aromatic rings. Recombinant TdnL retains these functional domains, allowing it to cleave toluene derivatives (e.g., toluene, xylene) into cis-dihydrodiol compounds, a key step in microbial degradation pathways.
Interest in TdnL stems from its biotechnological and industrial applications. It serves as a model enzyme for studying substrate specificity and catalytic mechanisms of dioxygenases, aiding in the rational design of enzymes for enhanced pollutant degradation. Additionally, its recombinant form is pivotal in synthetic biology for constructing microbial consortia tailored to detoxify contaminated environments. Recent studies also explore its potential in producing chiral synthons for pharmaceutical manufacturing.
Despite its utility, challenges persist in optimizing TdnL’s stability and activity under industrial conditions. Advances in protein engineering, such as directed evolution or fusion tags, aim to address these limitations. Overall, TdnL recombinant protein exemplifies the intersection of microbial biochemistry and applied biotechnology, offering sustainable solutions for environmental and chemical industries.
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