| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | alkB |
| Uniprot No | P05050 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-216aa |
| 氨基酸序列 | MLDLFADAEPWQEPLAAGAVILRRFAFNAAEQLIRDINDVASQSPFRQMVTPGGYTMSVAMTNCGHLGWTTHRQGYLYSPIDPQTNKPWPAMPQSFHNLCQRAATAAGYPDFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGLPAIFQFGGLKRNDPLKRLLLEHGDVVVWGGESRLFYHGIQPLKAGFHPLTIDCRYNLTFRQAGKKE |
| 预测分子量 | 44.1 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alkB重组蛋白的3篇参考文献示例(注：文献信息为模拟示例，实际引用时请核实原文)：
1. **文献名称**：*Cloning and Functional Characterization of alkB from Pseudomonas putida in Escherichia coli*
**作者**：van Beilen, J.B., et al.
**摘要**：该研究克隆了来自恶臭假单胞菌的alkB基因，并在大肠杆菌中成功表达。重组alkB蛋白表现出烷烃羟化酶活性，能催化C5-C12直链烷烃的羟基化，为烷烃代谢机制研究提供基础。
2. **文献名称**：*Crystal Structure of Recombinant alkB: Insights into Substrate Specificity*
**作者**：Nie, Y., et al.
**摘要**：通过X射线晶体学解析了重组alkB蛋白的三维结构，揭示了其活性位点中二铁中心的配位模式，阐明了其对中长链烷烃的底物选择性机制。
3. **文献名称**：*Optimized Expression of alkB in Bacillus subtilis for Bioremediation Applications*
**作者**：Chayabutra, C., & Wu, L.
**摘要**：研究通过优化启动子和培养条件，在枯草芽孢杆菌中高效表达重组alkB蛋白，证明其可有效降解石油污染中的烷烃类化合物，具有生物修复潜力。
如需具体文献，建议通过PubMed或Web of Science检索关键词“alkB recombinant protein”或结合研究领域进一步筛选。
**Background of AlkB Recombinant Protein**
The AlkB protein, originally identified in hydrocarbon-degrading bacteria such as *Pseudomonas* and *E. coli*, is a key enzyme involved in the oxidative metabolism of alkanes. As a member of the non-heme diiron monooxygenase family, AlkB catalyzes the hydroxylation of medium-chain alkanes (C₅–C₁₆), converting them into primary alcohols. This reaction initiates the degradation pathway, enabling bacteria to utilize alkanes as carbon and energy sources. Its activity is oxygen-dependent and requires electron transport components (e.g., rubredoxin and reductase) for function.
Recombinant AlkB refers to the protein produced via genetic engineering in heterologous expression systems like *E. coli* or yeast. Cloning the *alkB* gene into expression vectors allows large-scale production, facilitating biochemical and structural studies. Researchers often modify the protein with affinity tags (e.g., His-tags) to simplify purification. Recombinant AlkB has been instrumental in elucidating substrate specificity, catalytic mechanisms, and thermostability, with structural analyses revealing insights into its diiron active site and substrate-binding pockets.
Biotechnologically, AlkB holds promise in environmental remediation, particularly in biodegrading petroleum hydrocarbons. Its ability to oxidize alkanes makes it valuable for oil spill cleanup and wastewater treatment. Additionally, engineered AlkB variants are explored for industrial applications, such as biofuel production or synthesis of chiral alcohols. Challenges include optimizing activity toward longer alkanes, enhancing stability under harsh conditions, and improving electron transfer efficiency in synthetic systems.
Current research focuses on protein engineering (e.g., directed evolution) to expand AlkB’s substrate range and catalytic efficiency. Studies also investigate its role in synthetic biology for designing microbial consortia or metabolic pathways. Overall, AlkB recombinant protein serves as a versatile tool in both fundamental enzymology and applied biotechnology, bridging microbial ecology with sustainable industrial processes.
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