| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UCP1 |
| Uniprot No | P25874 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 232-267aa |
| 氨基酸序列 | PVDVVKTRFINSPPGQYKSVPNCAMKVFTNEGPTAF |
| 预测分子量 | 30 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篇关于UCP1重组蛋白研究的参考文献摘要，基于领域内典型研究方向整合而成：
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1. **文献名称**: *"Recombinant Expression and Functional Characterization of UCP1 in a Bacterial System"*
**作者**: Lee, J. et al.
**摘要**: 研究团队在大肠杆菌中成功表达并纯化了重组UCP1蛋白，验证了其质子泄漏活性。通过脂质体重建实验，证明重组UCP1在体外可恢复脂肪酸依赖性解偶联功能，为体外药物筛选提供了模型。
2. **文献名称**: *"Structural Insights into UCP1 Activation by Fatty Acids Using Cryo-EM"*
**作者**: García-Ruiz, E. et al.
**摘要**: 通过昆虫细胞体系表达人源重组UCP1.利用冷冻电镜解析其与花生四烯酸结合的高分辨率结构，揭示了脂肪酸结合域构象变化如何触发质子通道活性，为靶向UCP1的肥胖治疗奠定结构基础。
3. **文献名称**: *"Development of a Mammalian Cell Line for Stable Production of Functional UCP1"*
**作者**: Chen, X. & Harper, M.E.
**摘要**: 在HEK293细胞中建立稳定表达重组UCP1的细胞系，结合氧耗测定验证其增强线粒体解偶联的能力。该模型被用于高通量筛选UCP1激动剂，以探索其在代谢疾病中的治疗潜力。
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**注**：以上文献为示例性质，实际引用时需以真实发表的论文为准。近年来UCP1重组蛋白研究多聚焦于结构解析(如冷冻电镜技术)、活性调控机制及基于重组蛋白的药物开发平台构建。
Uncoupling Protein 1 (UCP1) is a mitochondrial inner membrane protein primarily expressed in brown adipose tissue (BAT), where it plays a central role in non-shivering thermogenesis. Discovered in the 1970s, UCP1 belongs to the family of mitochondrial anion carrier proteins and is uniquely specialized for heat production. It functions by dissipating the proton gradient across the mitochondrial membrane, uncoupling oxidative phosphorylation from ATP synthesis. This process generates heat instead of chemical energy, making BAT critical for maintaining body temperature in newborns and hibernating mammals.
The interest in UCP1 surged with findings linking its activity to energy expenditure and metabolic health. Studies in the 1990s demonstrated that UCP1-knockout mice lacked adaptive thermogenesis, confirming its essential role. Researchers later explored its potential relevance to obesity and metabolic disorders, as enhanced UCP1 activity could theoretically increase energy expenditure and reduce fat storage.
Recombinant UCP1 proteins are engineered using heterologous expression systems, such as *E. coli* or mammalian cell lines, to produce purified UCP1 for structural, functional, and pharmacological studies. These systems allow large-scale production of the protein while preserving its functional properties, such as proton transport and regulation by fatty acids or purine nucleotides. Advanced techniques like cryo-EM and X-ray crystallography have utilized recombinant UCP1 to resolve its structural dynamics and interaction mechanisms.
Current research focuses on leveraging recombinant UCP1 for drug discovery, particularly for metabolic syndrome, and bioengineering applications, including synthetic biology approaches to induce thermogenesis in non-BAT cells. Challenges remain in stabilizing the protein’s conformation *in vitro* and mimicking its native lipid membrane environment. Nonetheless, UCP1 remains a pivotal target for understanding and manipulating metabolic energy balance.
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