| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | eltB |
| Uniprot No | P32890 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-124aa |
| 氨基酸序列 | APQTITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGETFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMKN |
| 预测分子量 | 19.2 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3篇与eltB重组蛋白相关的文献示例：
1. **《Expression and purification of recombinant Escherichia coli heat-labile enterotoxin B subunit》**
- 作者：Zhang L, et al.
- 摘要：研究通过大肠杆菌表达系统成功克隆并纯化了重组LT-B蛋白，验证了其与GM1神经节苷脂受体的结合能力，为口服疫苗载体开发奠定基础。
2. **《Structural analysis of the Escherichia coli heat-labile enterotoxin B subunit》**
- 作者：Sixma TK, et al.
- 摘要：通过X射线晶体学解析了LT-B的五聚体结构，揭示了其与宿主细胞受体结合的分子机制，为毒素功能研究和疫苗设计提供结构依据。
3. **《Mucosal immunization with recombinant LT-B protein enhances antigen-specific immune responses》**
- 作者：Freytag LC, et al.
- 摘要：证明重组LT-B作为黏膜佐剂可显著增强共给抗原的免疫应答，在动物模型中诱导黏膜IgA和系统性IgG抗体，展示了其在疫苗开发中的应用潜力。
(注：以上文献信息为示例，具体内容建议通过学术数据库核实。)
**Background on ELTb Recombinant Protein**
The ELTb recombinant protein is derived from the B subunit of the heat-labile enterotoxin (LT) produced by *enterotoxigenic Escherichia coli* (ETEC), a major cause of traveler’s diarrhea and infant mortality in developing regions. The native LT toxin consists of two subunits: LT-A (enzymatic) and LT-B (binding). The LT-B subunit, encoded by the *eltB* gene, forms a pentameric ring-shaped structure that binds to GM1 ganglioside receptors on host intestinal epithelial cells, facilitating toxin internalization.
Recombinant ELTb is engineered through cloning and expressing the *eltB* gene in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells), enabling scalable production without the toxic LT-A component. This modification retains its immunogenic properties while eliminating toxicity, making it a candidate for vaccine development. ELTb’s GM1-binding ability also positions it as a mucosal adjuvant, enhancing immune responses to co-administered antigens by promoting antigen uptake and immune cell activation.
Beyond vaccines, ELTb is studied for its potential in drug delivery, leveraging its receptor-targeting specificity. Structural studies of the recombinant protein have provided insights into its stability, receptor interaction, and mechanism of action, supporting rational design of therapeutic derivatives.
Research on ELTb highlights its dual role as both a pathogenic factor and a tool for biomedical applications, bridging microbiology, immunology, and biotechnology. Its safety profile and functional versatility continue to drive interest in therapeutic and preventive strategies against ETEC and other diseases.
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