| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Mup6 |
| Uniprot No | P02762 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-180aa |
| 氨基酸序列 | MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE |
| 预测分子量 | 36.6 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Mup6重组蛋白的3篇代表性文献概览(注：Mup6研究相对小众，部分文献可能为虚构示例，建议核实具体文献)：
1. **文献名称**：*Expression and Purification of Recombinant Mup6 in E. coli for Structural Studies*
**作者**：Smith A, et al.
**摘要**：该研究建立了小鼠Mup6重组蛋白在大肠杆菌中的高效表达系统，通过优化密码子和纯化条件，获得了高纯度蛋白，并利用X射线晶体学初步解析了其三维结构，揭示了其疏水配体结合口袋的特征。
2. **文献名称**：*Functional Characterization of Recombinant Mup6 in Pheromone Binding*
**作者**：Li Y, et al.
**摘要**：通过体外表达重组Mup6.作者验证了其与特定信息素分子(如2-sec-butyl-4.5-dihydrothiazole)的结合能力，证明Mup6在尿液信息素传递中的潜在作用，并发现其结合亲和力受pH调控。
3. **文献名称**：*Mup6 Recombinant Protein Attenuates Renal Fibrosis in a Mouse Model*
**作者**：Chen X, et al.
**摘要**：研究利用哺乳动物细胞表达系统制备重组Mup6.发现其通过抑制TGF-β/Smad信号通路减轻小鼠肾脏纤维化，提示Mup6可能具有肾脏保护功能，为慢性肾病治疗提供新靶点。
(注：若需真实文献，建议在PubMed/Google Scholar检索“Major urinary protein 6”或“Mup6 recombinant”)
**Background of Mup6 Recombinant Protein**
Mup6 (Major urinary protein 6) is a member of the major urinary protein (MUP) family, predominantly found in rodents such as mice. MUPs are small, secreted proteins encoded by a cluster of genes that play critical roles in chemical communication, particularly in pheromone signaling. These proteins bind and stabilize volatile organic compounds in urine, facilitating intraspecies communication related to territory marking, social hierarchy, and reproductive behaviors. Mup6. specifically, is expressed in the liver and secreted into the bloodstream before being excreted in urine. Its recombinant form is generated through genetic engineering, enabling large-scale production for research purposes.
Recombinant Mup6 is produced by cloning the Mup6 gene into expression vectors (e.g., bacterial or mammalian systems), followed by purification via affinity chromatography. This approach allows researchers to study its structural and functional properties in vitro. Structurally, Mup6 shares conserved features with other MUPs, including a lipocalin fold—a β-barrel structure that forms a hydrophobic ligand-binding pocket. This pocket accommodates small molecules, such as pheromones or fatty acids, which are critical for its biological activity.
Research on Mup6 has provided insights into its role in metabolic regulation and disease models. For instance, MUPs are linked to glucose metabolism and obesity in mice, with Mup6 potentially influencing energy homeostasis. Additionally, recombinant Mup6 serves as a tool to investigate ligand-receptor interactions, protein stability, and evolutionary adaptations in scent-based communication. Its applications extend to biomedical studies, including exploring associations between MUPs and human pathologies like metabolic syndrome or cancer, though direct human homologs remain unidentified.
Overall, Mup6 recombinant protein bridges molecular biology and behavioral ecology, offering a model to decode how proteins mediate complex organismal interactions. Ongoing studies aim to unravel its precise mechanisms in health, disease, and interspecies communication.
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