| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | THI2.3 |
| Uniprot No | P32880 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-46aa |
| 氨基酸序列 | KSCCPNTTGRNIYNTCRFGGGSREVCASLSGCKIISASTCPSYPDK |
| 预测分子量 | 17.8 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3条关于THI2.3重组蛋白的虚构参考文献示例(注：THI2.3蛋白暂无明确对应真实研究，以下内容为模拟学术文献格式，仅供参考)：
1. **文献名称**：Expression and Functional Analysis of Recombinant THI2.3 Protein in Arabidopsis Stress Response
**作者**：Chen L., et al.
**摘要**：本研究成功在大肠杆菌系统中表达并纯化了THI2.3重组蛋白，实验表明该蛋白通过调节硫胺素代谢通路增强拟南芥对氧化胁迫的抗性，为植物抗逆机制提供了新见解。
2. **文献名称**：Structural Characterization of THI2.3 Recombinant Protein via X-ray Crystallography
**作者**：Rodriguez S., Kim H.
**摘要**：首次解析了THI2.3重组蛋白的三维晶体结构，揭示了其活性位点的保守性及与硫胺素前体结合的分子机制，为设计靶向代谢调控分子奠定基础。
3. **文献名称**：THI2.3 Recombinant Protein Enhances Fungal Pathogen Resistance in Crop Plants
**作者**：Wang Y., et al.
**摘要**：通过体外重组表达THI2.3蛋白并应用于小麦叶片实验，发现其能显著抑制病原真菌侵染，可能与激活植物系统抗性信号通路相关。
(提示：以上文献为模拟创作，实际研究中请通过学术数据库核实真实文献。)
**Background of THI2.3 Recombinant Protein**
THI2.3 (Thionin 2.3) is a small, cysteine-rich protein belonging to the plant thionin family, which is primarily associated with plant defense mechanisms. Thionins are antimicrobial peptides widely distributed in higher plants, known for their roles in combating pathogens, pests, and abiotic stresses. The THI2.3 gene, identified in *Arabidopsis thaliana*, encodes a cationic peptide characterized by a conserved structure stabilized by disulfide bonds. Unlike some thionins that exhibit broad-spectrum toxicity, THI2.3 is specifically implicated in responses to fungal pathogens and certain environmental stressors.
The recombinant THI2.3 protein is typically produced using heterologous expression systems, such as *Escherichia coli* or yeast, enabling large-scale purification for functional studies. Its recombinant form retains the bioactive properties of the native protein, including antimicrobial activity against phytopathogenic fungi and bacteria. Studies suggest that THI2.3 disrupts microbial cell membranes through electrostatic interactions, leading to cell lysis. Additionally, its expression in plants is regulated by jasmonate signaling, linking it to systemic acquired resistance.
Research on THI2.3 has focused on elucidating its role in plant innate immunity and stress adaptation. Its recombinant variant serves as a tool for exploring structure-function relationships, optimizing stability, and assessing potential applications in agricultural biotechnology, such as engineering disease-resistant crops. Despite its promise, challenges remain in balancing its antimicrobial efficacy with plant cytotoxicity, a common issue with thionins. Overall, THI2.3 exemplifies how plant-derived peptides can inspire sustainable strategies for crop protection, bridging fundamental plant science and biotechnological innovation.
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