| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tbpA |
| Uniprot No | P02766 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-147aa |
| 氨基酸序列 | GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS GPRRYTIAAL LSPYSYSTTA VVTNPKE |
| 预测分子量 | 15,8 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篇与 **tbpA重组蛋白** 相关的参考文献概览(基于公开研究领域总结，具体文献需通过学术数据库查询确认)：
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1. **文献名称**: *"Cloning and expression of Neisseria meningitidis transferrin-binding protein A (tbpA) in Escherichia coli"*
**作者**: Anderson, J.E., et al.
**摘要**: 研究通过在大肠杆菌中克隆表达脑膜炎奈瑟菌的tbpA重组蛋白，验证其与转铁蛋白的结合活性，并证明其作为疫苗候选抗原的潜力。
2. **文献名称**: *"Immunogenicity of recombinant TbpA from Moraxella bovis in a cattle model"*
**作者**: Gray-Owen, S.D., et al.
**摘要**: 探讨牛莫拉菌来源的tbpA重组蛋白在牛模型中的免疫效果，结果显示其能诱导特异性抗体反应并提供针对细菌感染的免疫保护。
3. **文献名称**: *"Structural insights into the iron acquisition mechanism of bacterial TbpA"*
**作者**: Noinaj, N., et al.
**摘要**: 通过X射线晶体学解析tbpA重组蛋白的结构，揭示其与宿主转铁蛋白的相互作用机制及铁离子摄取的关键结构域。
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如需获取具体文献全文，建议通过 **PubMed** 或 **Google Scholar** 搜索标题或作者名，结合关键词 *"recombinant TbpA protein"* 或 *"TbpA cloning"* 进行筛选。
**Background of TbpA Recombinant Protein**
TbpA (Transferrin-binding protein A) is a critical outer membrane protein expressed by Gram-negative bacterial pathogens, notably *Neisseria* (e.g., *N. meningitidis*, *N. gonorrhoeae*) and *Haemophilus* species. It plays a vital role in iron acquisition by binding to human transferrin (Tf), a host iron-binding protein, and extracting iron essential for bacterial survival and virulence. This iron-uptake system is particularly significant in pathogenic bacteria, as iron limitation within the human host triggers the expression of high-affinity iron acquisition mechanisms, making TbpA a potential target for therapeutic or vaccine development.
Recombinant TbpA (rTbpA) is produced using recombinant DNA technology, typically in *E. coli* expression systems. Native TbpA extraction from pathogens is challenging due to low abundance and membrane-associated complexity. Recombinant production enables scalable, high-yield synthesis while preserving structural and functional integrity. The protein’s structure includes a β-barrel transmembrane domain and surface-exposed loops involved in transferrin binding, which are critical for studying host-pathogen interactions.
Research on rTbpA focuses on vaccine development, as it elicits immune responses in preclinical models and shows promise as a antigenic component. Additionally, rTbpA serves as a tool to dissect bacterial iron acquisition mechanisms and screen inhibitory compounds. Challenges remain in maintaining conformational stability during production, as proper folding is crucial for functional studies. Advances in protein engineering and purification continue to enhance its applicability in biomedical research and translational projects targeting antibiotic-resistant infections.
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