| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | stxB2 |
| Uniprot No | P09386 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-89aa |
| 氨基酸序列 | ADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND |
| 预测分子量 | 14.7 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 **stxB2重组蛋白** 的示例参考文献，内容基于常见研究方向构造，仅供参考。建议通过学术数据库(如PubMed、Google Scholar)获取真实文献：
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1. **文献名称**: *Expression and Immunogenicity of Recombinant Shiga Toxin B Subunit Type 2 in a Murine Model*
**作者**: Zhang Y. et al.
**摘要**: 研究报道了在大肠杆菌中高效表达重组stxB2蛋白，并通过亲和层析纯化。实验证明该蛋白在小鼠模型中诱导了特异性抗体反应，提示其作为潜在疫苗候选分子的可能性。
2. **文献名称**: *Targeted Drug Delivery Using stxB2-Conjugated Nanoparticles for Gb3 Receptor-Rich Cancers*
**作者**: Wang L. et al.
**摘要**: 利用重组stxB2蛋白与纳米颗粒结合，靶向表达Gb3受体的乳腺癌细胞。实验显示，该载体系统显著提高了化疗药物的靶向性和抗肿瘤效果，同时减少对正常细胞的毒性。
3. **文献名称**: *Structural and Functional Characterization of Recombinant stxB2: Implications for Shiga Toxin Neutralization*
**作者**: Kumar S. et al.
**摘要**: 通过X射线晶体学解析重组stxB2的三维结构，并验证其与Gb3受体的结合位点。研究为设计基于stxB2的中和抗体或抑制剂提供了结构基础。
4. **文献名称**: *Development of an stxB2-Based ELISA for Rapid Detection of Shiga Toxin-Producing E. coli*
**作者**: Chen H. et al.
**摘要**: 开发了一种基于重组stxB2蛋白的ELISA检测方法，用于快速筛查食品和临床样本中的产志贺毒素大肠杆菌(STEC)，灵敏度高达95%，特异性优异。
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**备注**：上述文献为示例，实际研究中请查阅具体发表论文以获取准确信息。
**Background of StxB2 Recombinant Protein**
StxB2 is a subunit of Shiga toxin type 2 (Stx2), a bacterial exotoxin produced by certain strains of *Escherichia coli* (e.g., STEC or EHEC). The toxin comprises an enzymatically active A subunit (StxA) and a pentameric B subunit (StxB), with StxB2 specifically associated with the Stx2 variant. The B subunit mediates host cell binding by recognizing globotriaosylceramide (Gb3) receptors on cell surfaces, enabling toxin internalization. StxB2 itself lacks cytotoxic activity, making it a safer target for research and therapeutic applications compared to the holotoxin.
Recombinant StxB2 is engineered using expression systems like *E. coli* or yeast, allowing large-scale production with high purity. Its structure retains receptor-binding capability, enabling its use as a tool for studying toxin-host interactions, Gb3 receptor distribution, and intracellular trafficking mechanisms. Additionally, StxB2 has been explored in biomedical applications, such as drug delivery vectors (targeting Gb3-rich cancer cells) and vaccine development. For instance, it serves as an antigen in vaccines against EHEC infections or as an adjuvant to enhance immune responses.
Research on StxB2 also extends to diagnostics, where it aids in detecting Gb3-expressing cells or anti-Stx antibodies. Its non-toxic nature, coupled with specific targeting, underscores its versatility in both basic science and translational medicine. Ongoing studies focus on optimizing its stability, binding affinity, and compatibility with therapeutic platforms, reinforcing its potential in combating infectious diseases and cancer.
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