| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DPT |
| Uniprot No | Q07507 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-201aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHGNLYFQGGEFGQYGDYGYPYQQYHDYSDDGW VNLNRQGFSYQCPQGQVIVAVRSIFSKKEGSDRQWNYACMPTPQSLGEPT ECWWEEINRAGMEWYQTCSNNGLVAGFQSRYFESVLDREWQFYCCRYSKR CPYSCWLTTEYPGHYGEEMDMISYNYDYYIRGATTTFSAVERDRQWKFIM CRMTEYDCEFANV |
| 预测分子量 | 24 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DPT重组蛋白的3篇参考文献示例(部分为示例性描述，实际文献需根据具体研究验证)：
1. **文献名称**: "Recombinant expression and functional characterization of Dermatopontin (DPT) in extracellular matrix remodeling"
**作者**: Smith J, et al. (2021)
**摘要**: 研究通过大肠杆菌系统重组表达DPT蛋白，验证其促进胶原纤维组装的能力，并证明其在皮肤损伤修复中的潜在应用。
2. **文献名称**: "Development of a recombinant diphtheria toxin mutant as a vaccine antigen"
**作者**: Lee S, et al. (2020)
**摘要**: 利用重组技术表达无毒突变型白喉毒素(DT)，在小鼠模型中诱导高滴度中和抗体，为新一代白喉疫苗开发提供依据。
3. **文献名称**: "High-yield production of recombinant pertactin (PRN) from Bordetella pertussis and its immunogenicity analysis"
**作者**: Zhang Y, et al. (2019)
**摘要**: 通过昆虫细胞表达系统高效表达百日咳黏附素PRN，纯化后蛋白可诱导小鼠产生特异性抗体，支持其作为无细胞百日咳疫苗组分。
4. **文献名称**: "A trivalent DPT subunit vaccine based on recombinant proteins induces protective immunity in preclinical models"
**作者**: García R, et al. (2022)
**摘要**: 结合重组白喉类毒素、百日咳PT突变体及破伤风毒素C片段的三联疫苗，在动物实验中展现与传统灭活疫苗相当的免疫原性，且安全性更优。
**注意**：上述文献标题及摘要均为示例性质，实际研究中需根据具体内容检索真实文献(如通过PubMed或Web of Science)。建议使用关键词“recombinant DPT protein”、“dermatopontin expression”或“diphtheria-pertussis-tetanus subunit vaccine”进行精准检索。
**Background of DPT Recombinant Proteins**
Recombinant protein technology has revolutionized vaccine development, including for diphtheria, pertussis (whooping cough), and tetanus (DPT)—three historically devastating infectious diseases. Traditional DPT vaccines use inactivated or attenuated pathogens or toxoids (detoxified toxins). However, these formulations, particularly whole-cell pertussis vaccines, often cause adverse reactions due to residual virulence factors or impurities.
The emergence of recombinant DNA technology in the late 20th century enabled the production of **recombinant subunit vaccines**, which utilize purified antigenic proteins derived from pathogens. For DPT, this involves cloning genes encoding immunogenic proteins (e.g., pertussis toxin [PT], filamentous hemagglutinin [FHA], tetanus toxoid [TT], or diphtheria toxoid [DT]) into expression systems like *E. coli* or yeast. These systems produce large quantities of target proteins with high purity, minimizing nonessential pathogen components and improving safety profiles.
Recombinant DPT vaccines aim to address limitations of conventional vaccines. For example, acellular pertussis (aP) vaccines, containing recombinant PT, FHA, and other antigens, replaced whole-cell versions in many countries due to reduced side effects. Similarly, recombinant diphtheria and tetanus toxoids offer consistent quality and scalability compared to traditional toxin inactivation methods.
Challenges remain, such as ensuring recombinant proteins maintain proper conformational epitopes for immune recognition and balancing cost-effective production with stability. Nonetheless, advancements in structural biology, adjuvants, and delivery systems continue to enhance the efficacy of recombinant DPT vaccines. These innovations underscore the shift toward precision-engineered vaccines that prioritize safety, consistency, and adaptability against evolving pathogens.
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