| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | stxB |
| Uniprot No | P69179 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-89aa |
| 氨基酸序列 | TPDCVTGKVEYTKYNDDDTFTVKVGDKELFTNRWNLQSLLLSAQITGMTVTIKTNACHNGGGFSEVIFR |
| 预测分子量 | 13.3 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. |
以下是关于stxB(志贺毒素B亚基)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23 in HeLa cells"*
**作者**：Johannes L. et al.
**摘要**：该研究揭示了StxB亚基在细胞内运输机制，证明其与分子伴侣BiP及核仁蛋白B23的相互作用，为重组StxB在靶向药物递送中的应用提供了分子基础。
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2. **文献名称**：*"Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 Å resolution"*
**作者**：Fraser M.E. et al.
**摘要**：通过X射线晶体学解析了志贺毒素(含StxB亚基)的三维结构，阐明了B亚基与宿主细胞表面Gb3受体结合的机制，为重组StxB的设计优化提供了结构依据。
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3. **文献名称**：*"Targeting cancer cells with transferrin conjugates containing Shiga toxin B subunit"*
**作者**：Nishikawa K. et al.
**摘要**：研究利用重组StxB与转铁蛋白结合构建靶向载体，证实其选择性结合癌细胞表面受体并诱导凋亡，展示了其在肿瘤靶向治疗中的潜力。
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以上文献涵盖了StxB的结构解析、细胞内运输机制及治疗应用，均为该领域的代表性研究。如需具体发表年份或期刊信息，可进一步查询PubMed或相关数据库。
**Background of STxB Recombinant Protein**
The Shiga toxin B-subunit (STxB) is a non-toxic component of Shiga toxin, a bacterial protein produced by *Shigella dysenteriae* and certain enterohemorrhagic *Escherichia coli* (EHEC) strains. The holotoxin comprises an enzymatically active A-subunit (StxA) and a pentameric B-subunit (STxB), which mediates host cell binding. STxB specifically targets globotriaosylceramide (Gb3), a glycosphingolipid receptor overexpressed on certain cancer cells (e.g., colorectal, lymphoma) and endothelial cells in specific tissues.
Recombinant STxB, produced via genetic engineering in bacterial or eukaryotic expression systems, retains the receptor-binding capability without the cytotoxic effects of StxA. Its ability to bind Gb3 enables applications in targeted drug delivery, diagnostics, and vaccine design. For instance, STxB can shuttle conjugated antigens or therapeutics into cells via Gb3-mediated endocytosis, exploiting retrograde transport to reach the Golgi apparatus and endoplasmic reticulum. This pathway enhances antigen presentation, making STxB a valuable tool in immunotherapy.
In research, STxB is used to study intracellular trafficking, membrane dynamics, and Gb3-expressing cell behavior. Its non-toxic nature and high specificity also position it as a safe candidate for clinical exploration, particularly in oncology for targeting Gb3-rich tumors. Additionally, STxB-based vaccines against pathogens or tumors are under investigation, leveraging its immune-potentiating properties.
Overall, STxB recombinant protein exemplifies a versatile biomolecule bridging microbiology, cell biology, and translational medicine, offering promising avenues for precision therapies and molecular studies.
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