| 纯度 | >90%SDS-PAGE. |
| 种属 | MOUSE |
| 靶点 | MUP1 |
| Uniprot No | P11588 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-180aa |
| 氨基酸序列 | MKMLLLLCVG LTLVCVHAEE ASSTGRNFNV EKINGEWHTI ILASDKREKI EDNGNFRLFL EQIHVLENSL VLKFHTVRDE ECSELSMVAD KTEKAGEYSV TYDGFNTFTI PKTDYDNFLM AHLINEKDGE TFQLMGLYGR EPDLSSDIKE RFAQLCEKHG ILRENIIDLS NANRCLQARE |
| 预测分子量 | 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MUP1重组蛋白的参考文献示例(注：以下为假设性示例，实际文献需通过学术数据库验证)：
1. **"Heterologous Expression and Purification of Recombinant MUP1 in Escherichia coli"**
*Authors: Smith J., Brown A., et al. (2005)*
**摘要**: 本研究报道了在大肠杆菌中高效表达和纯化重组MUP1蛋白的优化方法，通过亲和层析和尺寸排阻色谱获得高纯度蛋白，并验证了其结构稳定性。
2. **"Crystal Structure Analysis of MUP1 Reveals Ligand-Binding Specificity"**
*Authors: Lee S., Kim H., et al. (2010)*
**摘要**: 通过X射线晶体学解析了重组MUP1的三维结构，揭示了其疏水口袋中配体(如信息素)的结合模式，为理解其在哺乳动物化学通讯中的作用提供结构基础。
3. **"Recombinant MUP1 Modulates Hepatic Lipid Metabolism in Mouse Models"**
*Authors: Johnson R., Patel D., et al. (2018)*
**摘要**: 利用重组MUP1蛋白进行体内实验，证明其通过调节肝脏FGF21信号通路影响脂质代谢，为代谢性疾病治疗提供潜在靶点。
4. **"Development of a MUP1-Based Fluorescent Biosensor for Small Molecule Screening"**
*Authors: Zhang L., Wang Q., et al. (2020)*
**摘要**: 基于重组MUP1的配体结合特性，构建了一种新型荧光生物传感器，用于高通量筛选与MUP1互作的小分子化合物，推动药物开发应用。
建议通过PubMed或Google Scholar以关键词“recombinant MUP1 protein”、“MUP1 expression”检索真实文献。
MUP1 (Major Urinary Protein 1) is a member of the lipocalin protein family, primarily studied in mice (Mus musculus). These small, secreted proteins are synthesized in the liver and excreted in urine, playing a critical role in chemical communication. MUP1 binds and transports hydrophobic pheromones, such as 2-sec-butyl-4.5-dihydrothiazole, which regulate social and reproductive behaviors in rodents. Its high concentration in urine—up to 30 mg/mL—makes it a key mediator of scent-based signaling, influencing territorial marking, mate attraction, and dominance hierarchies.
Structurally, MUP1 adopts a conserved lipocalin fold: an eight-stranded β-barrel enclosing a ligand-binding cavity. This hydrophobic pocket allows selective interaction with volatile organic compounds. Notably, MUPs exhibit polymorphism, with over 20 paralogs in mice, enabling diverse ligand-binding capacities. MUP1’s stability and resistance to proteolysis enhance its utility as a model for studying protein-ligand interactions and folding dynamics.
Recombinant MUP1 is typically produced in Escherichia coli or yeast expression systems, enabling large-scale studies. Researchers use it to dissect the structural basis of pheromone recognition, olfactory processing, and ligand-release mechanisms. Its recombinant form retains native binding properties, facilitating crystallography and NMR studies. Beyond behavioral biology, MUP1 has biomedical relevance as lipocalins are implicated in human diseases, including cancer and inflammation. Engineered MUPs also inspire biosensor designs for detecting environmental volatiles. Recent work explores its role in metabolic regulation, linking urinary proteins to energy homeostasis. Despite its murine origin, MUP1’s conserved features offer insights into evolutionary biology and interspecies communication strategies.
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