| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPR |
| Uniprot No | P35270 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-261aa |
| 氨基酸序列 | MEGGLGRAVCLLTGASRGFGRTLAPLLASLLSPGSVLVLSARNDEALRQLEAELGAERSGLRVVRVPADLGAEAGLQQLLGALRELPRPKGLQRLLLINNAGSLGDVSKGFVDLSDSTQVNNYWALNLTSMLCLTSSVLKAFPDSPGLNRTVVNISSLCALQPFKGWALYCAGKAARDMLFQVLALEEPNVRVLNYAPGPLDTDMQQLARETSVDPDMRKGLQELKAKGKLVDCKVSAQKLLSLLEKDEFKSGAHVDFYDK |
| 预测分子量 | 75.8 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SPR(表面等离子体共振)技术应用于重组蛋白研究的模拟参考文献示例，供参考：
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1. **文献名称**：Surface Plasmon Resonance Analysis of Recombinant Antibody-Antigen Interactions
**作者**：Karlsson, R., et al.
**摘要**：研究利用SPR技术定量分析重组单克隆抗体与靶标抗原的结合动力学(如亲和力Ka/Kd)，验证重组蛋白的功能性，为抗体药物开发提供数据支持。
2. **文献名称**：Optimizing Recombinant Protein Purification via SPR-Based Binding Assays
**作者**：Smith, J.P., & Lee, C.
**摘要**：通过SPR实时监测重组蛋白与亲和层析介质的结合效率，优化纯化工艺参数(如pH、离子强度)，提升蛋白产量与活性。
3. **文献名称**：SPR Screening of Recombinant Receptor-Ligand Interactions in Drug Discovery
**作者**：Zhang, Y., et al.
**摘要**：采用SPR高通量筛选重组表达的人源受体蛋白与候选药物分子的结合特异性，揭示小分子化合物的构效关系，加速先导化合物优化。
4. **文献名称**：Real-Time Analysis of Recombinant Protein Multimerization by SPR
**作者**：Müller, T., et al.
**摘要**：利用SPR技术动态监测重组蛋白(如病毒衣壳蛋白)的自组装过程，阐明多聚体形成机制及环境因素的影响。
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*注：以上为模拟文献，实际文献需通过PubMed、Web of Science等学术平台检索，关键词建议：SPR/Surface Plasmon Resonance, recombinant protein, kinetics, binding assay.*
**Background of SPR Recombinant Proteins**
Surface Plasmon Resonance (SPR)-based recombinant proteins are engineered molecules widely utilized in biomolecular interaction analysis. Recombinant proteins, produced via genetic engineering in host systems (e.g., bacteria, yeast, or mammalian cells), mimic native proteins with high purity and specificity. SPR technology, a label-free optical sensing method, enables real-time monitoring of molecular interactions by detecting refractive index changes near a sensor surface. When combined with recombinant proteins, SPR becomes a powerful tool for studying binding kinetics, affinity, and specificity between biomolecules (e.g., protein-ligand, antibody-antigen).
The development of SPR-compatible recombinant proteins has revolutionized drug discovery, immunology, and diagnostics. For instance, therapeutic antibodies or vaccine candidates are often analyzed using SPR to assess target engagement and optimize binding properties. Recombinant proteins tagged with affinity tags (e.g., His-tag, GST) simplify immobilization on SPR sensor chips, ensuring consistent experimental reproducibility.
SPR recombinant proteins also play a critical role in characterizing immune responses, such as profiling antibody-antigen interactions during infectious disease outbreaks or autoimmune disorders. Additionally, they are integral to quality control in biopharmaceutical manufacturing, verifying batch consistency and stability of biologics like monoclonal antibodies or enzyme replacement therapies.
Advancements in protein engineering, such as site-specific mutagenesis or fusion protein design, further enhance SPR assay sensitivity and specificity. These proteins are pivotal in personalized medicine, enabling rapid screening of patient-derived samples for tailored therapies. Overall, SPR recombinant proteins bridge structural biology and functional analytics, offering high-throughput, precise data to accelerate biomedical research and therapeutic development.
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