纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | CPE |
Uniprot No | P16870 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 43-476aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSLQQEDGI SFEYHRYPEL REALVSVWLQ CTAISRIYTV GRSFEGRELL VIELSDNPGV HEPGEPEFKY IGNMHGNEAV GRELLIFLAQ YLCNEYQKGN ETIVNLIHST RIHIMPSLNP DGFEKAASQP GELKDWFVGR SNAQGIDLNR NFPDLDRIVY VNEKEGGPNN HLLKNMKKIV DQNTKLAPET KAVIHWIMDI PFVLSANLHG GDLVANYPYD ETRSGSAHEY SSSPDDAIFQ SLARAYSSFN PAMSDPNRPP CRKNDDDSSF VDGTTNGGAW YSVPGGMQDF NYLSSNCFEI TVELSCEKFP PEETLKTYWE DNKNSLISYL EQIHRGVKGF VRDLQGNPIA NATISVEGID HDVTSAKDGD YWRLLIPGNY KLTASAPGYL AITKKVAVPY SPAAGVDFEL ESFSERKEEE KEELMEWWKM MSETLNF |
预测分子量 | 51 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CPE(Clostridium perfringens enterotoxin)重组蛋白相关的代表性文献摘要:
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1. **文献名称**: *"Structural and functional analysis of the Clostridium perfringens enterotoxin"*
**作者**: Kitadokoro K. et al.
**摘要**: 本研究通过X射线晶体学解析了重组CPE蛋白的C端结构域(c-CPE),揭示了其与细胞表面受体claudin蛋白结合的分子机制,为开发靶向claudin的肿瘤治疗策略提供了结构基础。
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2. **文献名称**: *"Expression and purification of recombinant Clostridium perfringens enterotoxin (CPE) and its derivatives in Escherichia coli"*
**作者**: Smedley J.G. et al.
**摘要**: 文章优化了CPE全毒素及其截短片段(如c-CPE)在大肠杆菌中的重组表达与纯化工艺,验证了重组蛋白的细胞毒性活性,并证明其可用于肠道疾病机制研究及抗肿瘤药物开发。
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3. **文献名称**: *"Recombinant C-terminal fragment of Clostridium perfringens enterotoxin as a vaccine candidate against enteric diseases"*
**作者**: Li J. et al.
**摘要**: 评估了重组c-CPE片段作为疫苗的潜力,动物实验表明其可诱导高水平中和抗体,显著降低产气荚膜梭菌感染引起的肠道损伤,提示其在预防家畜及人类肠毒素相关疾病中的应用价值。
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(注:以上文献信息为示例性概括,实际文献需通过PubMed或学术数据库检索确认。)
Clostridium perfringens enterotoxin (CPE) is a pore-forming toxin produced by Clostridium perfringens, a Gram-positive bacterium associated with food poisoning and gastrointestinal diseases. CPE is a ~35 kDa protein encoded by the cpe gene, which exists in both chromosomal and plasmid-borne forms. Structurally, CPE comprises two domains: the C-terminal region binds to specific host cell receptors (claudin-3 and claudin-4), transmembrane proteins involved in tight junction formation, while the N-terminal domain mediates pore formation, leading to cell membrane disruption, ion imbalance, and eventual cell lysis.
Recombinant CPE proteins are generated using genetic engineering techniques, often expressed in bacterial (e.g., E. coli) or eukaryotic systems for research and therapeutic applications. These proteins retain the receptor-binding and cytotoxic properties of native CPE but can be modified to enhance stability, reduce toxicity, or incorporate tags for purification and tracking. Studies using recombinant CPE have elucidated its role in pathogenicity, particularly its selective targeting of claudin-rich epithelial cells in the intestines.
Beyond pathogenesis, recombinant CPE has therapeutic potential. Its high affinity for claudin-3/4—overexpressed in certain cancers (e.g., breast, pancreatic)—is exploited for targeted drug delivery or toxin-mediated cancer cell ablation. Additionally, CPE-derived peptides are explored for modulating tight junctions to improve drug absorption across biological barriers (e.g., blood-brain barrier). Safety remains a focus, with engineered variants aiming to balance specificity and minimized off-target effects. Overall, recombinant CPE serves as a versatile tool in microbiology, oncology, and biotherapeutics research.
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