| 纯度 | >85%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | eco |
| Uniprot No | B7UFM3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-162aa |
| 氨基酸序列 | AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLESKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR |
| 预测分子量 | 23.5 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3篇与Eco(大肠杆菌)重组蛋白表达相关的经典文献摘要概述：
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1. **文献名称**：*Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes*
**作者**：Studier, F. W. et al.
**摘要**：提出利用T7 RNA聚合酶系统在大肠杆菌中高效表达重组蛋白的方法，通过调控T7启动子实现目标基因的高选择性表达，显著提高蛋白产量。
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2. **文献名称**：*Overview of bacterial expression systems for heterologous protein production*
**作者**：Terpe, K.
**摘要**：综述大肠杆菌等表达系统的优缺点，重点讨论启动子(如lac、T7)、载体设计和宿主菌株选择对重组蛋白可溶性及活性的影响。
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3. **文献名称**：*Recombinant protein expression in Escherichia coli: advances and challenges*
**作者**：Baneyx, F. & Mujacic, M.
**摘要**：分析大肠杆菌表达重组蛋白的常见问题(如包涵体形成)，提出优化策略(如分子伴侣共表达、培养条件调控)以提高可溶性和功能性蛋白产量。
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4. **文献名称**：*Advanced genetic strategies for recombinant protein expression in Escherichia coli*
**作者**：Sørensen, H. P. & Mortensen, K. K.
**摘要**：探讨密码子优化、融合标签(如His-tag)和分泌信号肽等遗传工程手段对改善大肠杆菌中重组蛋白表达效率的作用。
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这些文献涵盖了大肠杆菌重组蛋白表达的核心技术、优化策略及挑战，适合作为研究基础参考。
**Background of Eco Recombinant Proteins**
Recombinant proteins produced using *Escherichia coli* (E. coli), often termed "Eco recombinant proteins," have been foundational in biotechnology since the 1970s. The advent of genetic engineering enabled scientists to insert foreign genes into E. coli, leveraging its rapid growth, cost-effective cultivation, and well-characterized genetics to produce proteins of interest. This system became a cornerstone for research and industrial applications due to its scalability and simplicity compared to eukaryotic expression systems.
E. coli is particularly suited for producing prokaryotic or simple eukaryotic proteins that do not require post-translational modifications (e.g., glycosylation). Early milestones included the production of human insulin in 1978. which revolutionized diabetes treatment, and later, enzymes, vaccines, and therapeutic proteins like interferons. The development of engineered strains (e.g., BL21. Rosetta) and plasmid vectors (e.g., pET, pGEX) further optimized protein yield and solubility.
However, challenges persist. Complex eukaryotic proteins often misfold or form inclusion bodies in E. coli, necessitating refolding strategies or fusion tags. The lack of native modification systems also limits production of certain biologics, such as monoclonal antibodies. To address these, researchers have developed strategies like codon optimization, co-expression of molecular chaperones, and strain engineering.
Recent advancements in synthetic biology, CRISPR, and AI-driven protein design continue to enhance E. coli's utility. Innovations include engineered strains for non-canonical amino acid incorporation, improved secretion systems, and metabolic pathway tweaks to reduce metabolic burden. Eco recombinant proteins remain vital in drug discovery, industrial enzymology, and basic research, though competition from yeast, insect, and mammalian systems drives ongoing optimization.
In summary, E. coli-based recombinant protein production balances cost, speed, and versatility, maintaining its relevance despite limitations, supported by continuous technological refinements.
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