| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | cdtC |
| Uniprot No | Q46670 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-181aa |
| 氨基酸序列 | CSSSQDSANNQIDELGKENNSLFTFRNIQSGLMIHNGLHQHGRETIGWEIVPVKTPEEALVTDQSGWIMIRTPNTDQCLGTPDGRNLLKMTCNSTAKKTLFSLIPSTTGAVQIKSVLSGLCFLDSKNSGLSFETGKCIADFKKPFEVVPQSHLWMLNPLNTESPII |
| 预测分子量 | 25.7 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cdtC重组蛋白的3篇参考文献及其摘要内容：
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1. **标题**：*Functional characterization of the *Campylobacter jejuni* cdtC gene product as a novel antagonist of host cell cycle progression*
**作者**：Lara-Tejero M, Galán JE
**摘要**：研究通过重组表达CdtC蛋白，发现其与CdtB亚基协同作用，导致宿主细胞G2/M期周期阻滞，揭示了CdtC在毒素功能中的辅助作用。
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2. **标题**：*Purification and characterization of the recombinant subunits of the cytolethal distending toxin*
**作者**：Elwell CA, Dreyfus LA
**摘要**：在大肠杆菌中分别表达并纯化cdtA、cdtB、cdtC重组蛋白，证实CdtC单独不具毒性，但为毒素复合体与宿主细胞膜结合所必需。
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3. **标题**：*Crystal structure of the CdtC subunit of the cytolethal distending toxin*
**作者**：Nesić D, Hsu Y, Stebbins CE
**摘要**：通过X射线晶体学解析重组CdtC的三维结构，发现其具有独特的β-桶状结构，可能介导毒素亚基间的相互作用及细胞表面结合。
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以上文献聚焦于cdtC重组蛋白的功能、结构及其在毒素复合体中的作用机制。如需具体年份或期刊信息，可进一步补充检索。
**Background of cdtC Recombinant Protein**
The cytolethal distending toxin (CDT) is a bacterial virulence factor produced by various Gram-negative pathogens, including *Escherichia coli*, *Campylobacter spp.*, and *Helicobacter hepaticus*. It comprises three subunits: CdtA, CdtB, and CdtC, which collectively induce cell cycle arrest and apoptosis in eukaryotic cells. Among these, CdtC plays a critical role in toxin assembly and targeting. While CdtB acts as a nuclease that damages host DNA, CdtC facilitates toxin delivery by interacting with cell membrane components, such as cholesterol-rich lipid domains, to promote toxin internalization.
Recombinant cdtC protein is generated through genetic engineering, often expressed in *E. coli* or other heterologous systems, enabling studies on its structural and functional properties. Its production allows researchers to dissect the molecular mechanisms of CDT toxicity, particularly how CdtC collaborates with CdtA and CdtB to form holotoxin complexes. Additionally, recombinant cdtC serves as a tool for developing therapeutic interventions, such as neutralizing antibodies or subunit vaccines, to counteract CDT-mediated pathogenesis.
Research on cdtC also explores its potential role in chronic infections and immune evasion, as CDT-producing bacteria are linked to diseases like gastroenteritis, periodontitis, and certain cancers. Challenges in studying cdtC include ensuring proper folding and post-translational modifications in recombinant systems, which may affect its biological activity. Despite these hurdles, cdtC remains a focal point for understanding bacterial toxin dynamics and advancing antimicrobial strategies.
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