| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INS |
| Uniprot No | P01308 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-110aa |
| 氨基酸序列 | MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN |
| 预测分子量 | 11,9 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INS重组蛋白的3篇代表性文献，简要概括如下：
1. **"Expression in Escherichia coli of chemically synthesized genes for human insulin"**
- **作者**: Goeddel, D.V. 等 (1979)
- **摘要**: 该研究首次通过化学合成人胰岛素基因并在大肠杆菌中成功表达，实现了重组人胰岛素的规模化生产，为糖尿病治疗提供了新途径。
2. **"Production of human insulin in yeast and its purification"**
- **作者**: Markussen, J. 等 (1987)
- **摘要**: 探索利用酵母表达系统生产重组人胰岛素，开发了高效纯化工艺，证明酵母系统在胰岛素生产中的可行性与成本效益。
3. **"Recombinant DNA technology for the production of insulin analogs"**
- **作者**: Vajo, Z. & Duckworth, W.C. (2000)
- **摘要**: 综述了重组技术制备胰岛素类似物的进展，包括长效/速效类似物的设计与临床应用，推动了糖尿病个性化治疗的发展。
4. **"Optimization of recombinant insulin production in Escherichia coli"**
- **作者**: Baeshen, N.A. 等 (2014)
- **摘要**: 通过优化大肠杆菌的发酵条件、密码子使用及下游纯化流程，显著提高了重组胰岛素的产量与稳定性。
(注：以上文献信息为示例性概括，具体内容建议通过PubMed或学术数据库检索验证。)
**Background of Recombinant Insulin (INS) Protein**
Recombinant insulin (INS) is a biotechnologically engineered version of the human insulin hormone, critical for regulating blood glucose levels. Before the advent of recombinant DNA (rDNA) technology, insulin for therapeutic use was extracted from the pancreases of pigs and cattle. While effective, animal-derived insulin posed challenges, including limited supply, potential immunogenicity, and ethical concerns. The discovery of insulin’s structure in the 1950s and advancements in molecular biology in the 1970s paved the way for recombinant insulin production.
In 1978. scientists at Genentech and City of Hope National Medical Center achieved a breakthrough by inserting the human insulin gene into *Escherichia coli* (*E. coli*), enabling bacteria to synthesize proinsulin, which was later enzymatically processed into active insulin. This marked the first successful production of a recombinant human protein. By 1982. recombinant human insulin became the first FDA-approved therapeutic protein produced via rDNA technology, commercialized as Humulin by Eli Lilly. This innovation eliminated reliance on animal sources, ensuring a safer, more scalable, and consistent supply.
Recombinant insulin is produced by expressing the insulin gene in microbial (e.g., *E. coli*, yeast) or mammalian cell systems. The process involves fermenting engineered cells, purifying the protein, and modifying it into its bioactive form. Over time, engineered insulin analogs (e.g., insulin lispro, glargine) with optimized pharmacokinetics were developed to better mimic physiological insulin release.
Today, recombinant insulin remains a cornerstone of diabetes management, benefiting millions worldwide. Its development exemplifies the transformative potential of biotechnology in addressing medical needs, while ongoing research focuses on improving delivery methods (e.g., oral formulations) and production efficiency using novel expression systems.
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