纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | CTN |
Uniprot No | P53441 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-172aa |
氨基酸序列 | MQKYGSKKIG ATSATSSNKQ KVQIELTDEQ RQEIKEAFDL FDMDGSGKID AKELKVAMRA LGFEPKKEEI KKMISGIDNG SGKIDFNDFL QLMTAKMSEK DSHAEIMKAF RLFDEDDSGF ITFANLKRVA KDLGENMTDE ELREMIEEAD RSNQGQISKE DFLRIMKKTN LF |
预测分子量 | 19,6 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CTN重组蛋白的3篇示例文献(内容为示例性概括,非真实文献):
1. **《High-yield production of SARS-CoV-2 nucleocapsid protein (CTN) in E. coli for serological assay development》**
- **作者**: Li, X., Zhang, Y., & Chen, Q.
- **摘要**: 研究通过大肠杆菌表达系统高效表达SARS-CoV-2核衣壳蛋白(CTN),优化诱导条件后获得可溶性重组蛋白,并验证其用于COVID-19血清学检测的灵敏度和特异性,为诊断试剂开发提供基础。
2. **《Structural and functional characterization of recombinant CTN protein from hepatitis E virus》**
- **作者**: Wang, T., Liu, H., & Liang, C.
- **摘要**: 利用哺乳动物细胞表达系统表达HEV CTN重组蛋白,通过X射线晶体学解析其三维结构,揭示其与RNA结合的关键位点,并验证其在病毒组装中的功能,为抗病毒药物设计提供依据。
3. **《A novel CTN-based fusion protein enhances antitumor immunity in murine models》**
- **作者**: Gupta, R., Patel, S., & Kim, D.
- **摘要**: 设计并表达一种CTN与免疫刺激因子融合的重组蛋白,在黑色素瘤小鼠模型中验证其通过激活T细胞和树突状细胞抑制肿瘤生长的效果,为癌症免疫治疗提供新策略。
4. **《Optimization of CTN protein purification using a tag-free strategy》**
- **作者**: Müller, J., Schmidt, A., & Fischer, B.
- **摘要**: 提出一种无标签的CTN重组蛋白纯化方法,通过离子交换层析和尺寸排阻色谱联用,提高蛋白纯度和稳定性,降低生产成本,适用于大规模工业应用。
(注:以上文献名为示例,如需真实文献,建议通过PubMed或Google Scholar检索关键词如“recombinant CTN protein”、“SARS-CoV-2 nucleocapsid protein”等。)
CTN recombinant proteins, typically referring to recombinant forms of β-catenin or related catenin family proteins, are engineered to study their roles in cellular signaling and structural regulation. Catenins, including β-catenin, α-catenin, and p120-catenin, are critical for cell-cell adhesion and Wnt signaling pathways. β-catenin, the most extensively studied, acts as a dual-function protein: stabilizing cadherin-based adherens junctions at the plasma membrane and serving as a transcriptional co-activator in the nucleus upon Wnt pathway activation. Dysregulation of β-catenin is linked to cancers, developmental disorders, and fibrosis, making it a key therapeutic target.
Recombinant CTN proteins are produced using expression systems like E. coli, insect cells, or mammalian cells to ensure proper folding and post-translational modifications. These proteins enable mechanistic studies, such as mapping interaction domains with partners like E-cadherin, APC, or TCF/LEF transcription factors. They also facilitate drug discovery by screening inhibitors targeting β-catenin's nuclear interactions or stability. In structural biology, recombinant CTN proteins aid in resolving 3D conformations to design precision therapies.
Challenges in CTN recombinant production include solubility issues due to its unstructured regions and maintaining functional integrity during purification. Advanced tags (e.g., GST, His-tags) and refolding techniques are often employed. Applications extend to disease modeling, organoid research, and regenerative medicine, where Wnt/β-catenin signaling directs stem cell differentiation. Commercial CTN recombinant proteins are widely used in ELISA, Western blot controls, and functional assays, underscoring their versatility in both basic and translational research.
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