| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | dps |
| Uniprot No | P0C558 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-183aa |
| 氨基酸序列 | MTSFTIPGLSDKKASDVADLLQKQLSTYNDLHLTLKHVHWNVVGPNFIGVHEMIDPQVELVRGYADEVAERIATLGKSPKGTPGAIIKDRTWDDYSVERDTVQAHLAALDLVYNGVIEDTRKSIEKLEDLDLVSQDLLIAHAGELEKFQWFVRAHLESAGGQLTHEGQSTEKGAADKARRKSA |
| 预测分子量 | 36.3 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DPS重组蛋白的3篇代表性文献(示例为假设性描述，实际文献需根据具体研究查询)：
1. **文献名称**：*Structural and functional analysis of Dps protein in oxidative stress protection*
**作者**：Wolfgang Dröge, et al.
**摘要**：本研究解析了DPS重组蛋白的晶体结构，揭示其通过形成十二聚体复合物与DNA结合，在氧化应激条件下保护细菌基因组免受自由基损伤的分子机制。
2. **文献名称**：*Dps-mediated iron sequestration in Escherichia coli under starvation conditions*
**作者**：Sarah J. Aves, et al.
**摘要**：该文献证明DPS重组蛋白通过螯合游离铁离子减少羟基自由基生成，并在营养缺乏时维持细菌存活，强调了其在氧化应激和金属代谢中的双重功能。
3. **文献名称**：*Role of Dps in bacterial persistence and biofilm formation*
**作者**：Dmitry A. Traore, et al.
**摘要**：研究利用重组DPS蛋白进行功能实验，发现其通过物理性压缩DNA和调节基因表达，促进细菌生物膜形成及抗生素耐受性，为病原菌耐药机制提供了新视角。
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**说明**：以上为领域内典型研究方向示例，实际文献需通过PubMed、Web of Science等数据库以关键词"Dps protein, DNA protection, oxidative stress, recombinant Dps"检索。建议结合具体研究需求筛选近年高被引论文。
**Background of DPS Recombinant Proteins**
DPS (DNA-binding protein from starved cells) recombinant proteins are engineered versions of a conserved bacterial protein initially identified in *Escherichia coli* during nutrient starvation. First characterized in the 1990s, DPS plays a critical role in bacterial stress response, protecting genomic DNA from oxidative damage, nucleases, and other stressors. Structurally, DPS forms a dodecameric nanocage (12 subunits) with dual functionality: it binds DNA to compact it into a protective crystalline lattice and exhibits ferroxidase activity, converting toxic Fe²⁺ into inert Fe³⁺ to prevent hydroxyl radical formation via the Fenton reaction.
The development of recombinant DPS proteins leverages genetic engineering to express and purify these proteins in heterologous systems (e.g., *E. coli* or yeast). Recombinant technology enables scalable production, site-specific modifications, and functional tuning for biotechnological applications. For instance, engineered DPS variants may incorporate altered DNA-binding domains or enhanced stability for industrial use.
DPS recombinant proteins have gained attention in nanotechnology and biomedicine due to their self-assembling nanostructures, biocompatibility, and cargo-loading capacity. Applications include vaccine delivery platforms, drug encapsulation, biosensors, and bio-templates for metallic nanoparticle synthesis. Their ability to protect DNA under extreme conditions also inspires research into novel preservation strategies for biologics or synthetic biology systems.
Current studies focus on optimizing DPS scaffolds for targeted delivery, improving catalytic properties, and exploring ecological roles in microbial communities. As a bridge between microbial physiology and synthetic biology, DPS recombinant proteins exemplify how natural stress-adaptation mechanisms can be repurposed for innovative solutions in healthcare, environmental science, and materials engineering.
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