| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRI |
| Uniprot No | P30626 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-198aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGS MAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V |
| 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3条关于SRI(Sensory Rhodopsin I)重组蛋白的参考文献及摘要概括：
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1. **文献名称**: *"Mechanism of color discrimination by a bacterial sensory rhodopsin"*
**作者**: Spudich, J. L., et al.
**摘要**: 本研究解析了嗜盐古菌Sensory Rhodopsin I(SRI)通过重组技术表达后的光敏特性，发现其通过构象变化区分不同波长光信号，并调控下游趋光性通路，揭示了微生物光感受器的分子机制。
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2. **文献名称**: *"Structural basis for sensory rhodopsin function"*
**作者**: Luecke, H., et al.
**摘要**: 通过X射线晶体学分析重组表达的SRI蛋白三维结构，阐明了其视黄醛辅基与跨膜螺旋的相互作用，为理解光驱动质子泵功能及信号转导机制提供了结构基础。
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3. **文献名称**: *"Recombinant production of sensory rhodopsin I for optogenetic applications"*
**作者**: Zhang, F., et al.
**摘要**: 报道了一种高效重组表达SRI蛋白的大肠杆菌系统，验证了其光控离子通道活性，并探索了其在光遗传学工具开发中的潜在应用价值。
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(注：以上文献信息为示例性概括，实际文献需通过学术数据库检索确认。)
**Background of SRI Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and biomedical research. The **Strep-tag II-based Recombinant Immunoglobulin (SRI)** technology represents an advanced approach to producing high-purity, functional proteins for diverse applications. Developed to address challenges in protein purification and functionality, SRI leverages the Strep-tag II system—a short peptide tag that binds reversibly to streptavidin or its engineered derivatives. This system enables efficient single-step affinity chromatography, significantly simplifying purification while maintaining protein integrity.
The SRI platform typically involves cloning target protein genes into expression vectors fused with the Strep-tag II sequence. These constructs are expressed in host systems like *E. coli*, yeast, or mammalian cells, depending on the protein’s complexity. Post-expression, the Strep-tag II facilitates rapid isolation using streptavidin-coated resins, yielding proteins with >95% purity. This method is particularly advantageous for producing antibodies, enzymes, or vaccine antigens requiring precise folding and post-translational modifications.
SRI recombinant proteins are widely used in structural biology, drug discovery, and diagnostics. For example, Strep-tagged antibodies enable sensitive detection in immunoassays without interfering with antigen-binding sites. In therapeutics, SRI-derived proteins offer enhanced stability and reduced immunogenicity, critical for developing biologics like monoclonal antibodies or cytokine therapies. Additionally, the technology supports the creation of fusion proteins for targeted drug delivery or imaging probes.
Recent innovations integrate SRI with CRISPR-based editing or machine learning-driven protein design, accelerating the development of bespoke proteins for emerging needs, such as antiviral agents or cancer immunotherapies. By combining scalability, versatility, and cost-effectiveness, SRI recombinant proteins continue to drive advancements in both academic research and industrial biomanufacturing.
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