| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPIL1 |
| Uniprot No | Q9Y3C6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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. |
1. **"Recombinant protein production in bacterial host"**
*作者：Rosano GL, Ceccarelli EA*
摘要：综述了大肠杆菌等原核表达系统在重组蛋白生产中的技术要点，比较不同宿主系统的优缺点，并讨论优化策略(如密码子优化、融合标签设计)。
2. **"Advances in COVID-19 mRNA vaccine development using recombinant proteins"**
*作者：Polack FP, et al.*
摘要：探讨重组蛋白技术在新冠mRNA疫苗研发中的应用，重点分析刺突蛋白(S蛋白)的重组表达与免疫原性验证。
3. **"Strategies for high-level recombinant protein expression in E. coli"**
*作者：Terpe K*
摘要：系统总结提高大肠杆菌中重组蛋白表达量的方法，包括启动子选择、诱导条件优化及包涵体复性策略。
4. **"Affinity chromatography: A versatile tool for protein purification"**
*作者：Hage DS, et al.*
摘要：针对重组蛋白纯化的亲和层析技术(如His标签、GST标签)进行原理分析，并讨论新型层析介质的开发进展。
(注：以上文献名为示例性概括，实际文献需根据具体研究主题检索PubMed/Web of Science获取)
**Background of Recomcombinant Proteins**
Recombinant proteins are genetically engineered proteins produced by introducing specific DNA sequences into host organisms, enabling them to express foreign proteins. This technology emerged in the 1970s with breakthroughs in molecular cloning and gene expression systems. The first milestone was the production of human insulin in *E. coli* in 1978. replacing animal-derived insulin and revolutionizing biopharmaceuticals.
The process involves isolating a target gene, inserting it into a plasmid vector, and transferring it into a host (e.g., bacteria, yeast, or mammalian cells). Host cells then synthesize the protein, which is purified for use. Key advantages include scalability, customization (e.g., adding tags for purification), and the ability to produce humanized proteins with reduced immunogenicity.
Recombinant proteins have become indispensable in therapeutics (e.g., monoclonal antibodies, vaccines), research tools (e.g., enzymes, cytokines), and industrial applications (e.g., biofuel enzymes). Mammalian systems (e.g., CHO cells) are preferred for complex proteins requiring post-translational modifications, while prokaryotic systems (e.g., *E. coli*) offer cost-effective production for simpler proteins.
Challenges include optimizing expression yields, ensuring proper folding, and minimizing host-induced contaminants. Advances in synthetic biology, CRISPR editing, and AI-driven protein design are addressing these issues, expanding applications in personalized medicine and sustainable biomanufacturing. Today, recombinant proteins underpin over 50% of biologics, highlighting their critical role in modern science and healthcare.
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