| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NMU |
| Uniprot No | P48645 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 36-174aa |
| 氨基酸序列 | CRGAPILPQGLQPEQQLQLWNEIDDTCSSFLSIDSQPQASNALEELCFMI MGMLPKPQEQDEKDNTKRFLFHYSKTQKLGKSNVVSSVVHPLLQLVPHLH ERRMKRFRVDEEFQSPFASQSRGYFLFRPRNGRRSAGFI |
| 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NMU(神经介素U)重组蛋白的模拟参考文献示例，基于领域内常见研究方向总结概括，供参考：
---
1. **文献名称**：*Expression and purification of recombinant Neuromedin U in E. coli for functional studies*
**作者**：Smith J, et al.
**摘要**：该研究通过大肠杆菌表达系统成功制备了重组NMU蛋白，优化了纯化条件，并验证其体外激活NMUR2受体的生物活性，为后续药理研究提供基础。
2. **文献名称**：*Neuromedin U recombinant protein suppresses appetite and modulates energy expenditure in obese mice*
**作者**：Chen L, et al.
**摘要**：通过动物实验证明，注射重组NMU蛋白显著降低肥胖模型小鼠的摄食量，并增加能量消耗，提示其在代谢疾病治疗中的潜在应用价值。
3. **文献名称**：*Structural insights into NMU-receptor interaction via recombinant NMU mutagenesis*
**作者**：Wang Y, et al.
**摘要**：利用重组NMU蛋白的定点突变技术，结合分子动力学模拟，揭示了NMU与G蛋白偶联受体NMUR1结合的关键氨基酸位点，为靶向药物设计提供依据。
4. **文献名称**：*Recombinant Neuromedin U as a therapeutic agent in cancer-associated cachexia*
**作者**：Kim S, et al.
**摘要**：体外和临床试验表明，重组NMU蛋白能够逆转癌症恶病质模型的肌肉萎缩，其机制可能与抑制促炎因子信号通路相关。
---
**注**：以上内容为示例性概括，实际文献需通过学术数据库(如PubMed、Web of Science)检索具体发表文章。
**Background of NMU Recombinant Protein**
Neuromedin U (NMU) is a highly conserved neuropeptide first identified in the 1980s, playing diverse roles in physiological processes such as energy homeostasis, stress response, gastrointestinal motility, and inflammation. It exists in multiple isoforms across species, with human NMU primarily expressed as a 25-amino-acid peptide (NMU-25) and an 8-amino-acid truncated form (NMU-8). These variants bind to two G protein-coupled receptors (GPCRs), NMUR1 and NMUR2. which exhibit distinct tissue distributions—NMUR1 is predominantly found in peripheral tissues (e.g., gut, adipose), while NMUR2 localizes to the central nervous system.
Recombinant NMU protein is produced via genetic engineering, often using bacterial (e.g., *E. coli*) or mammalian expression systems, enabling large-scale synthesis for research and therapeutic exploration. Its production typically involves codon optimization, affinity tag fusion (e.g., His-tag), and rigorous purification (e.g., HPLC) to ensure bioactivity. Researchers utilize recombinant NMU to study receptor signaling pathways (e.g., cAMP inhibition, Ca²⁺ mobilization) and its physiological effects, including appetite regulation, metabolic modulation, and immune response coordination.
Notably, NMU has emerged as a potential therapeutic target for obesity, diabetes, and inflammatory disorders due to its anorexigenic and anti-inflammatory properties. However, challenges remain, such as optimizing receptor specificity and stability *in vivo*. Recent studies also explore NMU's role in cancer progression, with conflicting evidence suggesting both tumor-promoting and suppressive effects depending on context.
Overall, recombinant NMU serves as a critical tool for deciphering its multifaceted biology and advancing translational applications, though further structural and functional studies are needed to unlock its full therapeutic potential.
×
