| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Ile |
| Uniprot No | P08004 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4-200aa |
| 氨基酸序列 | QNNRSRNEYHSNRKNEPSYELQNAHSGLFHSSNEELTNRNQRYTNQNASMGSFTPVQSLQFPEQSQQTNMLYNGDDGNNNTINDNERDIYGGFVNHHRQRPPPATAEYNDVFNTNSQQLPSEHQYNNVPSYPLPSINVIQTTPELIHNGSQTMATPIERPFFNENDYYYNNRNSRTSPSIASSSDGYADQEARPILE |
| 预测分子量 | 26.6 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篇关于Ile重组蛋白的虚拟参考文献示例(基于常见研究方向概括，非真实文献)：
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1. **文献名称**: *Optimization of Recombinant Protein Expression in E. coli through Codon Usage and Ile Supplementation*
**作者**: Zhang, L. et al.
**摘要**: 研究通过优化大肠杆菌表达系统中异亮氨酸(Ile)密码子使用及培养基中Ile浓度，提高重组蛋白产量，发现Ile的补充显著改善蛋白可溶性和稳定性。
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2. **文献名称**: *Role of Isoleucine Residues in the Thermostability of Recombinant Enzymes*
**作者**: Tanaka, K. & Suzuki, M.
**摘要**: 通过定点突变技术分析Ile残基在重组酶热稳定性中的作用，证实特定位置的Ile替换可增强酶在高温下的活性保留。
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3. **文献名称**: *Production of Ile-tagged Recombinant Proteins for Targeted Drug Delivery*
**作者**: Patel, R. et al.
**摘要**: 开发了一种基于异亮氨酸标签(Ile-tag)的重组蛋白纯化系统，并证明该标签可提高蛋白质在靶向药物递送中的细胞穿透效率。
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注：以上为示例性内容，实际文献需通过PubMed、Web of Science等数据库检索关键词如“recombinant protein isoleucine”或“Ile residue protein engineering”获取。
**Background of Recombinant Proteins**
Recombinant proteins are engineered through recombinant DNA technology, enabling the production of specific proteins by introducing target genes into host organisms (e.g., bacteria, yeast, mammalian cells). This approach revolutionized biotechnology by allowing large-scale synthesis of proteins that are difficult to isolate from natural sources. The process involves cloning a gene of interest into an expression vector, transforming host cells, and optimizing conditions for protein expression. Post-translationally modified proteins often require eukaryotic systems (e.g., CHO cells), while simpler proteins (e.g., insulin) can be produced in prokaryotic systems like *E. coli*.
Recombinant proteins have diverse applications: therapeutics (e.g., monoclonal antibodies, vaccines), research tools (e.g., enzymes, cytokines), and industrial biocatalysts. For instance, recombinant human insulin replaced animal-derived insulin, improving diabetes treatment safety. Similarly, cytokines like interferons and interleukins (IL-2. IL-6) are used in immunotherapy and cancer treatment.
Challenges include ensuring proper protein folding, post-translational modifications, and minimizing host-cell contaminants. Advances in synthetic biology, CRISPR, and AI-driven protein design are enhancing yield, specificity, and scalability. Emerging areas include engineered antibodies for targeted therapies and recombinant viral vectors for gene therapy.
While "Ile recombinant protein" isn’t a standard term, it may refer to proteins containing isoleucine (Ile) residues critical for structure/function or interleukin (IL) proteins with typographical errors. Either way, recombinant technology remains pivotal in addressing medical and industrial demands, driving innovation in biomanufacturing and personalized medicine.
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