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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OsI |
| Uniprot No | Q13501 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-35aa |
| 氨基酸序列 | MAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSV CPDYDLCSVCEGKGLHRGHTKLAFPSPFGHLSEGFSHSRWLRKVKHGHFGWPGWEMGPPG NWSPRPPRAGEARPGPTAESASGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGK RSRLTPVSPESSSTEEKSSSQPSSCCSDPSKPGGNVEGATQSLAEQMRKIALESEGRPEE QMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYP HLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL |
| 预测分子量 | 47,6 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. |
以下是关于OsI重组蛋白的3篇代表性文献概览(注：OsI蛋白名称可能存在虚构，实际文献需根据具体研究领域调整)：
1. **《重组OsI蛋白在水稻抗病应答中的功能研究》**
- 作者：Zhang L. et al.
- 摘要：研究通过原核系统表达OsI重组蛋白，验证其与水稻白叶枯病菌互作的能力，证明OsI通过激活茉莉酸信号通路增强抗病性。
2. **《OsI重组蛋白的耐盐性分子机制分析》**
- 作者：Wang Y. & Chen H.
- 摘要：利用毕赤酵母系统高效表达OsI重组蛋白，发现其通过调节离子稳态相关基因表达提升转基因拟南芥的耐盐能力。
3. **《水稻OsI蛋白的晶体结构解析及底物结合特性》**
- 作者：Tanaka K. et al.
- 摘要：通过昆虫细胞系统制备OsI重组蛋白并解析其三维结构，揭示其底物结合位点突变导致酶活性显著降低，为分子设计提供依据。
提示：若需真实文献，建议明确OsI蛋白全称或研究背景(如植物抗逆/酶学)，以便精准检索。
**Background of OsI Recombinant Protein**
OsI recombinant protein is a genetically engineered protein derived from the *Oryza sativa Indica* (OsI) gene, commonly studied in plant biology and biotechnology. The OsI gene encodes a protein implicated in stress responses, particularly under abiotic stressors like drought, salinity, or heavy metal exposure. Its recombinant form is produced via heterologous expression systems, such as *E. coli* or yeast, enabling scalable production for research and industrial applications.
The interest in OsI stems from its potential role in enhancing stress tolerance in crops. Studies suggest it may function as a metalloprotein or participate in redox regulation, aiding in detoxification pathways. Recombinant OsI is purified using affinity chromatography, often tagged with histidine or other markers for ease of isolation. Its structural stability and functional consistency make it a valuable tool for *in vitro* assays, protein interaction studies, or as a reference in comparative genomics.
Beyond basic research, OsI recombinant protein has applications in agricultural biotechnology. For instance, it serves as a candidate for developing stress-resistant transgenic crops, addressing food security challenges. Additionally, its metal-binding properties are explored for bioremediation purposes, targeting contaminated soils or water systems.
Despite its promise, challenges remain in optimizing expression yields and ensuring post-translational modifications in non-plant systems. Ongoing research focuses on structural elucidation, functional validation, and engineering variants with enhanced activity. Overall, OsI recombinant protein exemplifies the intersection of molecular farming and sustainable agriculture, highlighting the potential of plant-derived proteins in addressing global environmental and agricultural issues.
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