| 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.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
×
