纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TDH |
Uniprot No | P20132 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-328aa |
氨基酸序列 | MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVVIVCGGSNISLAQLRALKEQLGMTNRLPK |
预测分子量 | 42.1 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TDH(耐热直接溶血素)重组蛋白相关的文献摘要示例:
1. **《Expression and Purification of Recombinant Thermostable Direct Hemolysin from Vibrio parahaemolyticus》**
- **作者**: Yamamoto, K., et al.
- **摘要**: 本研究在大肠杆菌中成功表达并纯化了重组TDH蛋白,通过优化诱导条件提高可溶性表达。纯化后的蛋白保留了天然溶血活性,为后续致病机制研究提供了工具。
2. **《Structural Analysis of Recombinant TDH by X-ray Crystallography》**
- **作者**: Zhang, Y., et al.
- **摘要**: 利用重组TDH蛋白解析了其三维晶体结构,揭示了溶血活性关键结构域,并发现钙离子结合位点对其热稳定性的调控作用,为抑制药物设计提供结构基础。
3. **《Development of a TDH-Specific ELISA Using Recombinant Antigen》**
- **作者**: Lee, S.H., et al.
- **摘要**: 开发基于重组TDH蛋白的高灵敏度ELISA检测方法,可特异性识别副溶血性弧菌感染样本中的TDH抗体,显著提升临床诊断效率。
注:以上文献为示例性内容,实际引用时需查询具体数据库(如PubMed/Google Scholar)获取真实发表信息。
**Background of TDH Recombinant Protein**
TDH (thermostable direct hemolysin) is a key virulence factor produced by *Vibrio parahaemolyticus*, a Gram-negative bacterium commonly associated with seafood-borne gastroenteritis. First identified in the 1960s, TDH is a pore-forming toxin that disrupts host cell membranes, leading to cell lysis, inflammation, and diarrhea. Its thermostability allows it to retain activity even after cooking, contributing to its role in foodborne illness. The *tdh* gene, encoding this toxin, is often used as a marker to identify pathogenic strains of *V. parahaemolyticus*.
Recombinant TDH protein is produced through genetic engineering, typically by cloning the *tdh* gene into expression systems like *E. coli*. This approach enables large-scale, purified TDH production while avoiding risks associated with handling live pathogenic bacteria. Recombinant TDH retains the biological and antigenic properties of the native toxin, making it invaluable for research and diagnostics.
Studies on recombinant TDH focus on understanding its structure-function relationships, mechanisms of cytotoxicity, and its role in bacterial pathogenesis. It is widely used to develop detection assays, such as ELISA, and to generate antibodies for diagnosing *V. parahaemolyticus* infections. Additionally, recombinant TDH serves as a critical antigen in vaccine development and a tool for screening potential inhibitors targeting its hemolytic activity.
Despite its pathogenic role, TDH’s unique properties have spurred interest in biotechnological applications, including its use as a model for studying pore-forming toxins. Ongoing research aims to balance its utility in diagnostics and therapeutics with strategies to mitigate its harmful effects during infections.
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