| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | uspF |
| Uniprot No | P37903 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MNRTILVPIDISDSELTQRVISHVEEEAKIDDAEVHFLTVIPSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKFKLPTDRVHVHVEEGSPKDRILELAKKIPAHMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR |
| 预测分子量 | 32.0 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. |
以下为虚构的uspF重组蛋白相关参考文献示例(仅供格式参考，非真实文献)：
1. **《Functional characterization of UspF in E. coli stress response》**
Smith A, et al.
摘要：研究了大肠杆菌uspF基因编码的重组蛋白在氧化应激中的调控作用，通过重组表达和体外酶活实验证明其参与硫醇代谢通路。
2. **《Crystal structure of recombinant UspF reveals a novel ATP-binding motif》**
Lee J, et al.
摘要：通过X射线晶体学解析uspF重组蛋白的三维结构，发现其C端存在新型ATP结合结构域，为功能机制提供结构基础。
3. **《Heterologous expression of uspF enhances bacterial tolerance to osmotic stress》**
Zhang Y, et al.
摘要：在枯草芽孢杆菌中异源表达重组UspF蛋白，显著提升菌株在高渗环境下的存活率，提示其作为胁迫响应元件的应用潜力。
4. **《UspF interacts with GroEL: A study using recombinant pull-down assays》**
Patel R, et al.
摘要：通过重组蛋白Pull-down实验证实UspF与分子伴侣GroEL的物理相互作用，暗示其在蛋白质折叠应激通路中的辅助功能。
注：以上文献为模拟生成，实际研究需通过PubMed/Google Scholar等平台检索关键词(如"uspF recombinant protein"、"UspF stress response")获取真实数据。
**Background of USPF Recombinant Protein**
The uspF gene encodes a universal stress protein (USP) commonly found in bacteria, including *Escherichia coli* and other enteric pathogens. USPs are a conserved family of proteins induced under diverse stress conditions, such as nutrient deprivation, oxidative stress, or extreme pH, enabling bacterial survival in hostile environments. UspF, in particular, has been linked to stress adaptation and virulence regulation in pathogenic strains. Its exact molecular mechanism remains under investigation, but studies suggest it may interact with cellular pathways involved in stress signaling, biofilm formation, or metabolic adjustments during host infection.
Recombinant UspF protein is produced via genetic engineering, where the uspF gene is cloned into expression vectors (e.g., plasmid systems) and expressed in host organisms like *E. coli*. This allows large-scale purification of the protein for functional studies. The recombinant form retains the native protein’s structural and functional properties, enabling researchers to explore its biochemical interactions, structural features, and role in bacterial physiology.
Interest in UspF stems from its potential applications in antimicrobial research. As a stress-response mediator, it could serve as a target for novel therapeutics aimed at disrupting bacterial survival mechanisms. Additionally, recombinant UspF is used to study host-pathogen interactions, particularly how pathogens evade immune defenses or adapt to stressors during infection. Its role in virulence also makes it a candidate for vaccine development, where it might act as an antigen to elicit protective immune responses.
Overall, UspF recombinant protein serves as a valuable tool for deciphering bacterial stress adaptation and developing strategies to combat antibiotic-resistant infections. Ongoing research continues to uncover its precise biological functions and therapeutic potential.
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