| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PT |
| Uniprot No | Q6ISU1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-281aa |
| 氨基酸序列 | MAGTWLLLLLALGCPALPTGVGGTPFPSLAPPIMLLVDGKQQMVVVCLVLDVAPPGLDSPIWFSAGNGSALDAFTYGPSPATDGTWTNLAHLSLPSEELASWEPLVCHTGPGAEGHSRSTQPMHLSGEASTARTCPQEPLRGTPGGALWLGVLRLLLFKLLLFDLLLTCSCLCDPAGPLPSPATTTRLRALGSHRLHPATETGGREATSSPRPQPRDRRWGDTPPGRKPGSPVWGEGSYLSSYPTCPAQAWCSRSALRAPSSSLGAFFAGDLPPPLQAGAA |
| 预测分子量 | 29,2 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PT(百日咳毒素)重组蛋白的3篇示例参考文献(注：文献信息为示例性概括，实际引用请查询具体数据库获取真实文献)：
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1. **文献名称**：*"Expression and Purification of Recombinant Pertussis Toxin in Escherichia coli for Vaccine Development"*
**作者**：Xiao Y., et al. (2018)
**摘要**：研究通过在大肠杆菌中克隆并表达PT的S1亚基基因，优化表达条件以提高可溶性蛋白产量，并验证其免疫原性，为无细胞百日咳疫苗的研发提供基础。
2. **文献名称**：*"Structural Analysis of Recombinant Pertussis Toxin via Cryo-EM Reveals Key Functional Domains"*
**作者**：Smith J., Patel R. (2020)
**摘要**：利用冷冻电镜技术解析重组PT的三维结构，阐明其亚基组装机制和酶活性位点，为靶向抑制剂的开发提供结构生物学依据。
3. **文献名称**：*"Recombinant PT as a Novel Adjuvant in Cancer Immunotherapy: Enhancing T-cell Responses In Vivo"*
**作者**：Chen L., et al. (2021)
**摘要**：探索重组PT作为免疫佐剂的潜力，实验表明其可增强抗原特异性T细胞活化，在黑色素瘤小鼠模型中显著抑制肿瘤生长。
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**建议**：实际研究中请通过PubMed、Web of Science等平台检索最新文献，关键词如“recombinant pertussis toxin”、“PT protein expression”或结合具体研究方向(如结构、疫苗、免疫调节)。
**Background of PT Recombinant Protein**
Pertussis toxin (PT), a key virulence factor produced by *Bordetella pertussis*, the causative agent of whooping cough, has been extensively studied for its role in pathogenesis and immune modulation. PT is an AB₅-type exotoxin composed of a catalytic A subunit (S1) and a pentameric B subunit (S2–S5), which facilitates host cell entry by binding to surface receptors. Its enzymatic activity involves ADP-ribosylation of Gαi proteins, disrupting cellular signaling pathways and contributing to symptoms like lymphocytosis and impaired immune responses.
The development of recombinant PT (rPT) emerged with advancements in genetic engineering and protein expression systems. Traditional PT purification from *B. pertussis* cultures posed challenges, including low yield, contamination risks, and residual toxicity. Recombinant DNA technology enabled the production of rPT in heterologous hosts (e.g., *E. coli* or mammalian cells), allowing precise control over protein structure and function. Detoxified rPT, achieved through site-directed mutagenesis (e.g., replacing catalytic residues like Arg-9 or Glu-129), retains immunogenicity without toxicity, making it suitable for acellular pertussis vaccines (e.g., DTaP).
Beyond vaccines, rPT serves as a critical tool in biomedical research. It is used to study G protein-coupled receptor (GPCR) signaling, immune cell regulation, and intracellular trafficking mechanisms. The ability to produce modified or tagged variants (e.g., fluorescent or His-tagged rPT) further expands its experimental applications.
Efforts to optimize rPT production focus on enhancing stability, solubility, and post-translational modifications (e.g., proper disulfide bond formation) to mimic native PT. Today, rPT exemplifies the intersection of microbial pathogenesis, vaccinology, and biotechnology, highlighting its dual role as a therapeutic target and a versatile research reagent.
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