| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPN |
| Uniprot No | P16150 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-253aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSSTTAVQT PTSGEPLVST SEPLSSKMYT TSITSDPKAD STGDQTSALP PSTSINEGSP LWTSIGASTG SPLPEPTTYQ EVSIKMSSVP QETPHATSHP AVPITANSLG SHTVTGGTIT TNSPETSSRT SGAPVTTAAS SLETSRGTSG PPLTMATVSL ETSKGTSGPP VTMATDSLET STGTTGPPVT MTTGSLEPSS GASGPQVSSV KLSTMMSPTT STNASTVPFR NPDENSR |
| 预测分子量 | 26 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SPN重组蛋白的3篇参考文献示例，基于常见研究方向构建：
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1. **文献名称**: "Expression and Immunogenicity of Recombinant Streptococcus pneumoniae Surface Protein N (SPN) in Escherichia coli"
**作者**: Smith, J.R., et al.
**摘要**: 本研究成功在大肠杆菌中表达了重组SPN蛋白，优化了纯化工艺。通过小鼠模型证实重组SPN能诱导高滴度抗体，提示其作为疫苗候选的潜力。
2. **文献名称**: "Structural Characterization of Recombinant SPN via Cryo-Electron Microscopy Reveals Key Epitopes for Antibody Binding"
**作者**: Zhang, Y., et al.
**摘要**: 利用冷冻电镜技术解析了重组SPN的三维结构，识别出与宿主细胞结合的关键结构域，为基于结构的疫苗设计提供理论依据。
3. **文献名称**: "Evaluation of Recombinant SPN as a Diagnostic Antigen for Pneumococcal Infection Serology"
**作者**: Lee, H., & Patel, R.
**摘要**: 将重组SPN作为抗原开发ELISA检测试剂，临床样本验证显示其高敏感性和特异性，适用于肺炎链球菌感染的快速诊断。
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**注**：以上文献为示例性质，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。若需具体文献，建议提供SPN的全称或相关研究背景以进一步缩小范围。
**Background of SPN Recombinant Proteins**
Recombinant proteins, including SPN (Surface Protein N) or other context-specific variants, are engineered through genetic modification to express target proteins in heterologous host systems like *E. coli*, yeast, or mammalian cells. This technology emerged in the 1970s with advances in molecular cloning and gene expression tools, enabling scalable production of proteins with high purity and consistency.
SPN, depending on its biological context, may refer to specific functional proteins. For instance, in pathogenic bacteria like *Staphylococcus aureus* or *Streptococcus pneumoniae*, SPN often denotes surface-exposed proteins involved in host-pathogen interactions, immune evasion, or virulence. Recombinant SPN proteins are synthesized by cloning the encoding gene into expression vectors, followed by purification for research or therapeutic applications.
These proteins are pivotal in vaccine development, diagnostic assays, and structural studies. For example, SPN antigens can be used to generate antibodies for serological tests or as vaccine candidates to elicit protective immunity. Additionally, recombinant SPN facilitates mechanistic studies of protein function, such as ligand-receptor binding or enzymatic activity, without requiring native pathogen cultivation, enhancing biosafety.
The production of SPN recombinant proteins offers advantages over traditional extraction methods, including batch-to-batch consistency, reduced contamination risks, and the ability to modify proteins (e.g., adding tags for purification or solubility). Challenges include optimizing expression conditions to ensure proper folding and post-translational modifications, particularly for eukaryotic SPN proteins requiring mammalian systems.
Overall, SPN recombinant proteins represent a cornerstone of modern biotechnology, bridging basic research and clinical applications, with ongoing innovations in expression systems and engineering further expanding their utility.
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