| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DHN1 |
| Uniprot No | P12951 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-139aa |
| 氨基酸序列 | MEYQGQHGHATDKVEEYGQPVAGHGGFTGGPTGTHGAAGVGGAQLQATRDGHKTDGVLRRSGSSSSSSSEDDGVGGRRKKGMKEKIKEKLPGGAHKDAAGQQQQTAMAGEYAGTHGTEATGEKKGVMDKIKEKLPGGQH |
| 预测分子量 | 18.2 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DHN1重组蛋白的3篇代表性文献概览(注：以下内容为模拟示例，具体文献需通过学术数据库检索确认)：
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1. **文献名称**: *Functional characterization of recombinant DHN1 protein in drought stress tolerance*
**作者**: Smith, J.R., et al.
**摘要**: 本研究通过在大肠杆菌中重组表达植物来源的DHN1蛋白，发现其在体外能有效抑制脱水引起的酶活性丧失。实验证明DHN1通过结合水分子和稳定细胞膜结构，显著提升转基因酵母的耐旱性。
2. **文献名称**: *Structural insights into the disordered nature of DHN1 by NMR spectroscopy*
**作者**: Zhang, L., et al.
**摘要**: 利用核磁共振技术分析重组DHN1蛋白的结构，揭示其内在无序区域(IDRs)在低温胁迫下的构象变化。结果表明，IDRs通过动态相互作用与脂质双分子层结合，增强植物细胞低温适应性。
3. **文献名称**: *Overexpression of recombinant DHN1 in maize enhances salt stress resistance*
**作者**: Lee, H., et al.
**摘要**: 将重组DHN1基因导入玉米，发现其过表达显著提高植株的盐胁迫耐受性。生理学数据表明，DHN1通过调节活性氧(ROS)清除和离子稳态，减少盐诱导的氧化损伤。
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**提示**：建议通过PubMed、Google Scholar等平台以“DHN1 recombinant protein”或“Dehydrin1 heterologous expression”为关键词检索最新文献，重点关注植物逆境生理学或蛋白结构研究领域。
**Background of DHN1 Recombinant Protein**
Dehydrin 1 (DHN1), a member of the late embryogenesis abundant (LEA) protein family, is a stress-responsive protein predominantly found in plants. It plays a critical role in protecting cellular structures under abiotic stress conditions, such as drought, salinity, and cold. Dehydrins are characterized by conserved Y-segments and lysine-rich motifs, which contribute to their function as molecular chaperones by stabilizing membranes, proteins, and nucleic acids during dehydration.
Recombinant DHN1 is produced using genetic engineering techniques, where the *DHN1* gene is cloned into expression vectors (e.g., bacterial or yeast systems) and expressed in heterologous hosts like *Escherichia coli*. This allows large-scale production of the protein for functional studies. The recombinant form often includes affinity tags (e.g., His-tag) to facilitate purification via chromatography.
Research on DHN1 focuses on its structural properties, such as intrinsic disorder and phosphorylation-dependent interactions, which enable adaptive responses to environmental stress. Studies also explore its potential in agricultural biotechnology to enhance crop resilience. For instance, transgenic plants overexpressing DHN1 exhibit improved tolerance to water deficit and osmotic stress. Additionally, recombinant DHN1 serves as a tool to investigate its biochemical interactions with ligands like metals or DNA, shedding light on its protective mechanisms at the molecular level.
The development of DHN1 recombinant protein underscores its importance in both basic research and biotechnological applications, offering insights into plant stress adaptation and paving the way for engineering climate-resilient crops.
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