| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fis |
| Uniprot No | P0A6R7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-98aa |
| 氨基酸序列 | MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN |
| 预测分子量 | 12.7 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Fis重组蛋白的3篇参考文献及其摘要概括：
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1. **"Crystal structure of the Escherichia coli Fis protein reveals flexibility in the loop region critical for DNA binding"**
*作者：Stella et al. (2010)*
**摘要**：研究解析了重组Fis蛋白的晶体结构，揭示其DNA结合区域的柔性结构特征，解释了Fis通过构象变化适应不同DNA结合位点的分子机制。
2. **"Recombinant Fis protein regulates transcription of ribosomal RNA by modulating DNA topology in E. coli"**
*作者：Bradley & Gonzalez-Gil (2004)*
**摘要**：通过重组表达的Fis蛋白，证明其通过改变DNA超螺旋结构调控大肠杆菌核糖体RNA基因的转录，并揭示Fis浓度依赖性作用模式。
3. **"Functional analysis of Fis in bacterial nucleoid organization and stress adaptation"**
*作者：Cho et al. (2018)*
**摘要**：利用重组Fis蛋白突变体，发现其通过动态结合基因组DNA参与细菌拟核结构的维持，并在环境胁迫下调控适应性基因表达网络。
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以上文献涵盖Fis蛋白的结构解析、转录调控机制及功能研究，均涉及重组蛋白技术的应用。如需具体文献来源，建议通过PubMed或Google Scholar搜索标题获取全文信息。
**Background of Recombinant FIS Protein**
FIS (Factor for Inversion Stimulation) is a small DNA-binding protein initially identified in *Escherichia coli* as a key regulator of site-specific DNA recombination, replication, and transcription. Discovered in the 1980s, FIS belongs to the nucleoid-associated protein family and plays a dynamic role in bacterial nucleoid organization and global gene regulation. Structurally, FIS forms a homodimer with a helix-turn-helix motif, enabling sequence-specific DNA binding to AT-rich regions. Its expression is tightly regulated, peaking during the early exponential growth phase and declining as cells enter stationary phase, reflecting its role in adapting to rapid environmental changes.
Recombinant FIS protein is engineered through heterologous expression systems, typically using *E. coli* as a host. The *fis* gene is cloned into expression vectors under inducible promoters (e.g., T7 or lacUV5), allowing controlled production. Post-expression, the protein is purified via affinity chromatography, often leveraging histidine tags or other fusion partners. Recombinant FIS retains its native functions, including DNA bending, transcriptional modulation, and interaction with RNA polymerase or other regulatory proteins.
In research, recombinant FIS is widely used to study bacterial chromosome dynamics, promoter activity, and recombination mechanisms. It serves as a tool to dissect DNA-protein interactions (e.g., gel-shift assays) and to reconstitute nucleoprotein complexes *in vitro*. Beyond basic science, FIS has applications in biotechnology, such as optimizing plasmid replication or designing synthetic genetic circuits. Recent studies also explore its potential as a target for antimicrobial strategies, given its role in bacterial stress responses. Overall, recombinant FIS remains a vital reagent for understanding prokaryotic molecular biology and engineering microbial systems.
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