| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTP4A3 |
| Uniprot No | O75365 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-173aa |
| 氨基酸序列 | MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM |
| 预测分子量 | 19.5 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TP(Treponema pallidum)重组蛋白研究的模拟参考文献示例，涵盖不同研究方向：
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1. **文献名称**: *"Evaluation of Recombinant Tp47 Antigen for Serodiagnosis of Syphilis"*
**作者**: Zhang, L., et al.
**摘要**: 研究利用重组Tp47蛋白开发ELISA检测方法，证实其敏感性(98%)和特异性(99%)，优于传统非特异性检测，适用于梅毒血清学筛查。
2. **文献名称**: *"Immunogenicity of TP Recombinant Proteins Tp17 and Tp45 in Murine Models"*
**作者**: Liu, Y., Wang, C.
**摘要**: 通过在大肠杆菌中表达Tp17和Tp45.发现二者可诱导小鼠产生高滴度IgG抗体，提示其作为梅毒疫苗候选抗原的潜力。
3. **文献名称**: *"Rapid Detection of Syphilis Using TP Recombinant Protein-Based Lateral Flow Immunoassay"*
**作者**: Gupta, R., et al.
**摘要**: 开发基于重组Tp15蛋白的侧流层析试纸条，10分钟内完成检测，灵敏度达95%，适用于资源匮乏地区的即时诊断。
4. **文献名称**: *"Structural Insights into TP Recombinant Protein Tp0326 and Its Role in Pathogenesis"*
**作者**: Johnson, M.T., et al.
**摘要**: 通过晶体学解析Tp0326蛋白结构，揭示其与宿主细胞外基质的相互作用机制，为靶向药物设计提供依据。
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**注**: 上述文献为模拟示例，实际研究需参考具体数据库(如PubMed、ScienceDirect)。建议结合关键词“Treponema pallidum recombinant protein”或“TP antigen”检索真实文献。
**Background of TP Recombinant Protein**
TP recombinant protein refers to a genetically engineered protein derived from *Treponema pallidum*, the bacterium responsible for syphilis. The development of recombinant DNA technology in the late 20th century enabled the precise cloning, expression, and purification of pathogen-specific proteins, offering advantages over traditional antigen preparation methods, which often faced challenges like low purity and cross-reactivity.
Researchers identified key immunogenic antigens from *T. pallidum*, such as TpN15. TpN17. and TpN47. and cloned their genes into expression systems (e.g., *E. coli* or yeast). These systems produce large quantities of TP recombinant proteins with high specificity, minimizing non-target protein contamination. Purification techniques like affinity chromatography further enhance product consistency.
TP recombinant proteins are pivotal in syphilis diagnostics. They serve as antigens in serological assays (e.g., ELISA, Western blotting) to detect anti-*T. pallidum* antibodies, improving test accuracy and enabling differentiation between active and past infections. Additionally, they are explored as vaccine candidates to elicit targeted immune responses. Beyond applications, these proteins aid in studying *T. pallidum* biology, including host-pathogen interactions and mechanisms of immune evasion.
Despite their utility, challenges remain, such as ensuring proper protein folding post-expression and scaling production cost-effectively. Ongoing research focuses on optimizing expression systems and structural modifications to enhance immunogenicity. Overall, TP recombinant proteins represent a critical tool in combating syphilis, bridging gaps in diagnostics, therapeutics, and fundamental research.
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