| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IAA |
| Uniprot No | P26945 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-153aa |
| 氨基酸序列 | MPNVTIARES PLQDAVVQLI EELDRYLGDL YPAESNHLLD LQTLAKPDIR FLVARRSGTV VGCGAIAIDT EGGYGEVKRM FVQPTARGGQ IGRRLLERIE DEARAAGLSA LLLETGVYQA TRIALYRKQG FADRGPFGPY GPDPLSLFME KPL |
| 预测分子量 | 16,8 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IAA(吲哚乙酸)重组蛋白研究的3篇代表性文献的示例(内容为虚构，仅作格式参考)：
1. **文献名称**: "Expression and Functional Analysis of Recombinant IAA Protein in *Arabidopsis thaliana*"
**作者**: Smith J, et al.
**摘要**: 本研究通过构建IAA重组蛋白表达载体，利用大肠杆菌系统高效表达并纯化IAA蛋白。功能验证表明，重组IAA蛋白显著促进拟南芥根系的伸长，为植物激素作用机制提供了新证据。
2. **文献名称**: "Optimization of IAA Recombinant Protein Production in *E. coli* Using Response Surface Methodology"
**作者**: Wang L, Zhang H.
**摘要**: 通过响应面法优化IAA重组蛋白在大肠杆菌中的表达条件，包括诱导温度、IPTG浓度和培养时间，最终将蛋白产量提高3.2倍，为规模化生产提供了技术基础。
3. **文献名称**: "Structural Characterization of Recombinant IAA-Binding Protein in Plant Stress Response"
**作者**: Gonzalez R, et al.
**摘要**: 通过X射线晶体学解析了重组IAA结合蛋白的三维结构，揭示了其与IAA分子互作的关键氨基酸位点，并证明该蛋白在干旱胁迫下调控植物IAA信号通路的分子机制。
(注：以上文献及内容均为模拟生成，实际研究中请参考真实发表的学术论文。)
Indole-3-acetic acid (IAA), a primary auxin in plants, regulates growth and development processes such as cell elongation, root initiation, and tropic responses. As a naturally occurring plant hormone, IAA has been extensively studied since its discovery in the 1930s. However, the complexity of its biosynthesis pathways and rapid metabolic turnover in plants have driven interest in engineered alternatives. Recombinant IAA-related proteins emerged as critical tools to address these challenges, enabled by advances in genetic engineering and protein expression systems.
The development of recombinant IAA proteins gained momentum in the late 20th century with the identification of key enzymes in IAA biosynthesis, including tryptophan aminotransferases and flavin monooxygenases. Researchers began cloning corresponding genes into microbial hosts like *E. coli* or yeast for large-scale protein production. These recombinant systems overcome limitations in plant-extracted proteins, offering higher purity, scalability, and customization potential. Fusion tags (e.g., His-tag) are frequently incorporated to facilitate purification.
Current applications span agricultural biotechnology (e.g., biofertilizers), plant physiology research (auxin signaling studies), and industrial enzyme production. Recent innovations focus on engineering chimeric proteins that combine IAA biosynthesis enzymes with regulatory domains for controlled activity. Challenges remain in maintaining protein stability and biological activity in field conditions. Ongoing research explores optimized codon usage, thermostable variants, and nanoparticle delivery systems to enhance practical utility. As synthetic biology tools advance, recombinant IAA proteins are increasingly used as modular components in complex genetic circuits for precision agriculture.
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