| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PIR |
| Uniprot No | O00625 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-290aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSSKKVTLSVLSREQSEGVGARVRRSIGR PELKNLDPFLLFDEFKGGRPGGFPDHPHRGFETVSYLLEGGSMAHEDFCG HTGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRSSEKMVEPQ YQELKSEEIPKPSKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDPGA KHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDSVQVEN KDPKRSHFVLIAGEPLREPVIQHGPFVMNTNEEISQAILDFRNAKNGFER AKTWKSKIGN |
| 预测分子量 | 34 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. |
以下是几篇关于PIR(Protein Immune Response或重组蛋白技术)相关的示例性参考文献(内容为虚构，仅作格式参考)：
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1. **文献名称**：*"Efficient Expression and Purification of PIR Recombinant Protein in Escherichia coli"*
**作者**：Zhang, L. et al.
**摘要**：研究通过优化大肠杆菌表达系统，成功实现了PIR重组蛋白的高效可溶性表达，并通过亲和层析技术获得高纯度蛋白，为后续免疫学研究提供基础材料。
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2. **文献名称**：*"Structural and Functional Analysis of PIR Domain in Recombinant Fusion Proteins"*
**作者**：Smith, J.R. & Tanaka, K.
**摘要**：通过X射线晶体学解析PIR结构域的3D构象，揭示了其与免疫受体结合的分子机制，并验证了重组融合蛋白在体外炎症模型中的调控功能。
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3. **文献名称**：*"PIR-Based Recombinant Antigen for Serodiagnosis of Autoimmune Diseases"*
**作者**：Wang, Y. et al.
**摘要**：开发了一种基于PIR重组蛋白的ELISA检测试剂，可特异性识别患者血清中的自身抗体，显著提高了类风湿关节炎的诊断灵敏度和特异性。
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4. **文献名称**：*"Mammalian Cell Expression System Enhances Glycosylation of PIR Recombinant Protein"*
**作者**：Lee, S.H. et al.
**摘要**：比较哺乳动物细胞(CHO)与原核系统表达的PIR蛋白差异，证实CHO系统可保留天然糖基化修饰，显著增强蛋白的体内稳定性和免疫原性。
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注：以上文献为示例，实际研究中需检索PubMed、Google Scholar等数据库获取真实文献。若需具体领域文献，建议补充PIR蛋白的全称或研究背景。
**Background of PIR Recombinant Proteins**
PIR (Properly-folded Immunodominant Regions) recombinant proteins are engineered biomolecules designed to mimic specific antigenic regions of pathogens or target proteins while ensuring proper structural folding. This technology emerged from the need to produce highly immunogenic and functional proteins for vaccines, therapeutic agents, and diagnostic tools. Traditional recombinant protein production often faces challenges like misfolding, aggregation, or loss of native conformation, which can reduce biological activity or immune recognition. PIR strategies address these issues by focusing on preserving critical epitopes or functional domains through advanced molecular design.
The development of PIR proteins leverages genetic engineering tools to isolate and express immunodominant regions within heterologous systems, such as *E. coli*, yeast, or mammalian cells. For example, in vaccine design, PIR-based antigens derived from viral surface proteins (e.g., HPV L1 protein) are optimized to form virus-like particles (VLPs) that trigger robust immune responses without infectious risks. Similarly, in cancer therapy, PIR-engineered proteins can target tumor-specific antigens with high precision.
Key advantages include enhanced stability, reduced cross-reactivity, and scalability for industrial production. Advances in structural biology, computational modeling, and high-throughput screening have further refined PIR design, enabling customization for specific applications. However, challenges remain, such as ensuring post-translational modifications in non-mammalian systems and balancing immunogenicity with safety.
Overall, PIR recombinant proteins represent a versatile platform in biotechnology, bridging gaps between native protein complexity and practical manufacturability, with broad implications for infectious disease control, oncology, and personalized medicine.
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