纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | CTH |
Uniprot No | P32929 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-405aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS |
预测分子量 | 47 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CTH(胱硫醚酶)重组蛋白研究的模拟参考文献示例(实际文献需通过学术数据库查询):
1. **《重组人胱硫醚酶(CTH)在大肠杆菌中的高效表达与活性分析》**
- 作者:张伟等
- 摘要:研究通过优化大肠杆菌表达系统,成功表达并纯化了具有酶活性的重组人CTH蛋白,证实其在体外可催化胱硫醚转化为半胱氨酸及α-酮丁酸,为硫化氢代谢研究提供工具。
2. **《CTH重组蛋白的晶体结构解析及其催化机制研究》**
- 作者:Chen, L. 等
- 摘要:利用X射线晶体学首次解析了CTH重组蛋白的三维结构,揭示了其底物结合位点及催化关键氨基酸残基,阐明了CTH在硫化氢生物合成中的分子机制。
3. **《酵母表达系统中CTH重组蛋白的分泌表达及功能验证》**
- 作者:Wang, Y. 等
- 摘要:采用毕赤酵母系统实现CTH的分泌表达,纯化蛋白在细胞模型中恢复了胱硫醚代谢功能,证实其在治疗高胱氨酸尿症等代谢疾病中的潜在应用价值。
4. **《CTH重组蛋白在神经退行性疾病模型中的保护作用》**
- 作者:Smith, J. 等
- 摘要:通过体外实验证明,重组CTH可通过调节硫化氢水平减轻氧化应激诱导的神经元损伤,提示其在阿尔茨海默病等神经退行性疾病中的治疗潜力。
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**提示**:以上为模拟示例,实际文献建议通过PubMed、ScienceDirect或Google Scholar检索关键词“CTH recombinant protein”“cystathionase expression”等获取。
**Background of CTH Recombinant Protein**
CTH recombinant protein is a genetically engineered fusion protein designed for biomedical research and therapeutic applications. The acronym "CTH" typically refers to a chimeric construct combining functional domains from distinct proteins, often to leverage synergistic properties. For instance, in vaccine development, CTH may integrate antigenic epitopes from pathogens (e.g., viral or bacterial proteins) with immunostimulatory molecules to enhance immune recognition and response.
A prominent example is the CTH construct derived from *Cholera Toxin B subunit* (CTB) fused with target antigens, such as human papillomavirus (HPV) E6/E7 oncoproteins. CTB serves as a mucosal adjuvant and delivery vehicle, improving antigen uptake by immune cells via its affinity for GM1 ganglioside receptors. Meanwhile, the fused antigens aim to elicit specific immune responses against infections or cancers. This design capitalizes on CTB’s safety profile and proven adjuvant effects, while the antigenic components drive targeted immunity.
CTH recombinant proteins are produced using expression systems like *E. coli* or yeast, ensuring cost-effective scalability. Their applications span prophylactic vaccines (e.g., HPV, Helicobacter pylori), therapeutic cancer vaccines, and diagnostic tools for detecting pathogen-specific antibodies. Preclinical studies highlight their ability to induce robust humoral and cellular immunity, particularly in mucosal tissues, making them promising for diseases transmitted via mucosal routes.
Challenges include optimizing stability, minimizing unintended immune reactions, and ensuring clinical efficacy. Ongoing research focuses on refining fusion designs, exploring novel adjuvants, and evaluating delivery platforms (e.g., nanoparticles) to enhance immunogenicity. Overall, CTH recombinant proteins represent a versatile strategy bridging immunology and genetic engineering, with potential to address unmet needs in infectious diseases and oncology.
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