| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STX2 |
| Uniprot No | P32856 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-288aa |
| 氨基酸序列 | MRDRLPDLTACRKNDDGDTVVVVEKDHFMDDFFHQVEEIRNSIDKITQYVEEVKKNHSIILSAPNPEGKIKEELEDLNKEIKKTANKIRAKLKAIEQSFDQDESGNRTSVDLRIRRTQHSVLSRKFVEAMAEYNEAQTLFRERSKGRIQRQLEITGRTTTDDELEEMLESGKPSIFTSDIISDSQITRQALNEIESRHKDIMKLETSIRELHEMFMDMAMFVETQGEMINNIERNVMNATDYVEHAKEETKKAIKYQSKARRKKWIIIAVSVVLVAIIALIIGLSVGK |
| 预测分子量 | 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STX2(志贺毒素2型)重组蛋白的3篇参考文献示例(注：文献信息基于研究领域常见主题推断，具体内容建议通过学术数据库进一步验证)：
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1. **文献名称**：*"Production and characterization of a recombinant Shiga toxin 2 (Stx2) protein for antibody generation"*
**作者**：Watanabe, A. et al.
**摘要**：该研究通过大肠杆菌表达系统成功表达并纯化了重组STX2蛋白，验证了其抗原性，并利用该蛋白制备了特异性单克隆抗体，为STX2感染的诊断和免疫学研究提供了工具。
2. **文献名称**：*"A recombinant chimeric protein-based vaccine against Shiga toxin 2-producing Escherichia coli"*
**作者**：Paton, A.W. & Paton, J.C.
**摘要**：研究者构建了包含STX2关键表位的重组嵌合蛋白，并在小鼠模型中评估其免疫保护效果。结果显示该蛋白能诱导中和抗体，显著降低毒素引起的病理损伤。
3. **文献名称**：*"Structural and functional analysis of Shiga toxin 2 (Stx2) receptor binding subunit"*
**作者**：Tesh, V.L. et al.
**摘要**：通过重组表达STX2的B亚基(Stx2B)，分析其与宿主细胞表面Gb3受体的相互作用机制，揭示了毒素内吞途径的关键结构域，为抑制毒素活性的药物设计提供依据。
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**注意**：以上文献信息为模拟示例，实际研究需通过PubMed、Google Scholar等平台检索具体文献(关键词：*recombinant Stx2 protein, Shiga toxin 2 expression*)。如需精准文献，可提供数据库访问权限进一步筛选。
**Background of STX2 Recombinant Protein**
Shiga toxin 2 (STX2), a key virulence factor produced by Shiga toxin-producing *Escherichia coli* (STEC), is associated with severe gastrointestinal and systemic complications, including hemorrhagic colitis and hemolytic uremic syndrome (HUS). Structurally, STX2 comprises an enzymatically active A subunit (StxA2) and a pentameric B subunit (StxB2). The B subunit facilitates toxin binding to globotriaosylceramide (Gb3) receptors on host cells, enabling the A subunit to inhibit protein synthesis via ribosomal RNA cleavage, leading to cell death.
Recombinant STX2 proteins are engineered using genetic cloning techniques, often expressed in *E. coli* or mammalian cell systems. These proteins retain functional or structural features of native STX2. depending on the design (e.g., full-length, subunit-specific, or mutated variants). Recombinant production allows controlled study of STX2’s mechanisms, bypassing the risks of handling live pathogens.
Research applications include vaccine development, therapeutic antibody testing, and diagnostic tool design. Recombinant STX2 subunits serve as antigens in serological assays to detect STEC infections or as standards in toxin quantification. Additionally, they aid in studying host-pathogen interactions, such as Gb3 receptor dynamics and intracellular trafficking.
Safety remains a priority; recombinant STX2 is often inactivated or modified to reduce cytotoxicity while preserving antigenicity. Regulatory guidelines ensure safe handling, given its association with life-threatening diseases.
Overall, recombinant STX2 proteins are pivotal in advancing diagnostics, therapeutics, and mechanistic insights into STEC-related pathologies, underscoring their importance in public health and biomedical research.
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