| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | III |
| Uniprot No | Q9BT43 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MASRGGGRGRGRGQLTFNVEAVGIGKGDALPPPTLQPSPLFPPLEFRPVPLPSGEEGEYVLALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPRELKIRVRKLQKERITILLPKRPPKTTEDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEEEEEEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY |
| 预测分子量 | 25,3 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篇与III型重组蛋白(可能与III型分泌系统或重组蛋白技术相关)相关的文献示例(注：文献信息为示例格式，非真实引用，仅供格式参考)：
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1. **文献名称**: "Structural insights into the assembly of the type III secretion needle complex"
**作者**: Schmidt, H., et al.
**摘要**: 该研究通过冷冻电镜解析了沙门氏菌III型分泌系统针状复合体的高分辨率结构，揭示了其组装机制及与宿主细胞膜互作的关键蛋白结构域。
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2. **文献名称**: "Recombinant type III effector proteins as tools in plant-pathogen interaction studies"
**作者**: Lee, J., et al.
**摘要**: 探讨利用重组表达的III型分泌效应蛋白(如来自丁香假单胞菌)在植物-病原体互作模型中的功能分析，验证其调控宿主免疫反应的分子机制。
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3. **文献名称**: "Development of a recombinant protein-based vaccine targeting Pseudomonas aeruginosa type III secretion system"
**作者**: Smith, R.P., & Johnson, A.
**摘要**: 研究通过重组表达铜绿假单胞菌III型分泌系统关键抗原蛋白(如PcrV)，开发新型亚单位疫苗，动物实验显示其可显著提高宿主对细菌感染的免疫保护。
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如需真实文献，建议通过PubMed、Google Scholar等平台检索关键词：**Type III secretion system recombinant protein** 或 **Recombinant protein expression type III**。
**Background of Type III Recombinant Proteins**
Type III recombinant proteins are engineered biomolecules primarily derived from bacterial type III secretion systems (T3SS), which are needle-like appendages used by pathogenic bacteria (e.g., *Salmonella*, *Shigella*) to inject effector proteins directly into host cells. These systems play a critical role in bacterial pathogenesis by manipulating host cell functions. Recombinant type III proteins, often produced via heterologous expression in *E. coli* or yeast systems, mimic key components of this machinery, such as effector proteins, translocators, or structural subunits.
The interest in type III recombinant proteins stems from their dual applications in basic research and therapeutic development. Structurally, they enable studies on host-pathogen interactions, including mechanisms of immune evasion and cellular hijacking. For instance, purified effector proteins are used to dissect signaling pathways they disrupt in host cells. Additionally, their immunogenic properties make them candidates for subunit vaccines, aiming to elicit protective immunity against bacterial infections.
Recent advances in protein engineering, such as codon optimization and fusion tags, have improved the solubility and stability of these recombinant proteins, addressing historical challenges in their production. Furthermore, synthetic biology approaches now allow the design of attenuated type III systems for targeted drug delivery or cancer immunotherapy, leveraging their ability to penetrate eukaryotic cells.
Despite progress, challenges remain, including maintaining conformational fidelity during *in vitro* production and minimizing endotoxin contamination. Ongoing research focuses on optimizing expression systems and functional validation in disease models. Overall, type III recombinant proteins represent a versatile toolset bridging microbiology, immunology, and biotechnology, with untapped potential for innovative therapies.
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