纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Enho |
Uniprot No | Q6UWT2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 34-76aa |
氨基酸序列 | CHSRSAD VDSLSESSPN SSPGPCPEKA PPPQKPSHEG SYLLQP |
预测分子量 | 7,9 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Enho重组蛋白的假设性参考文献示例(仅供参考,实际文献需通过学术数据库验证):
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1. **文献名称**:*Recombinant Adropin Protein Improves Glucose Homeostasis in Diet-Induced Obese Mice*
**作者**:Kumar, R. et al.
**摘要**:本研究利用大肠杆菌表达系统成功制备了重组Adropin蛋白,并验证其在糖尿病模型小鼠中的代谢调节作用。实验表明,重组Adropin可显著降低血糖水平并增强胰岛素敏感性。
2. **文献名称**:*Expression and Functional Characterization of ENHO-Derived Peptide in Hepatic Lipid Metabolism*
**作者**:Chen, L. & Wong, S.
**摘要**:通过哺乳动物细胞系表达ENHO基因编码的重组Adropin蛋白,发现其能够抑制肝细胞中脂质合成相关基因的表达,提示其在非酒精性脂肪肝治疗中的潜在应用。
3. **文献名称**:*Structural Insights into Adropin: A Circular Dichroism Study of Recombinant Protein*
**作者**:Zhang, Y. et al.
**摘要**:首次报道了重组Adropin蛋白的二级结构特征,利用圆二色光谱分析揭示其α-螺旋主导的构象,为理解其与受体相互作用提供了结构基础。
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**注意事项**:
- 上述文献为示例性质,实际研究中请通过PubMed、Web of Science等平台检索真实文献。
- 可尝试关键词:"Adropin recombinant production"、"ENHO protein expression" 或 "recombinant ENHO peptide function"。
- ENHO基因的研究多聚焦于代谢疾病(如糖尿病、肥胖),重组蛋白相关研究常涉及体外活性验证或动物模型应用。
Enho recombinant protein is derived from the energy homeostasis-associated (ENHO) gene, which encodes a secreted peptide hormone known as adropin. Discovered in 2008. adropin plays a critical role in regulating metabolic homeostasis, insulin sensitivity, and energy expenditure. It is primarily expressed in the liver and brain but also detected in tissues like the heart, kidneys, and adipose tissue. Structurally, adropin is a 76-amino-acid protein with a conserved N-terminal region and a variable C-terminal domain, contributing to its functional versatility in metabolic processes.
Research highlights adropin's involvement in lipid and glucose metabolism. It enhances glucose uptake in skeletal muscle, suppresses hepatic glucose production, and modulates lipid oxidation, making it a potential therapeutic target for metabolic disorders such as obesity and type 2 diabetes. Additionally, adropin influences cardiovascular health by improving endothelial function and reducing atherosclerosis risk.
Recombinant Enho protein is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems, ensuring proper folding and bioactivity. Its therapeutic potential is under investigation, with preclinical studies suggesting benefits in metabolic syndrome, non-alcoholic fatty liver disease (NAFLD), and cardiovascular diseases. Furthermore, adropin levels in circulation correlate with metabolic health, positioning it as a potential biomarker for disease progression or treatment response. Despite promising findings, further research is needed to fully elucidate its mechanisms and evaluate clinical applications. Enho recombinant protein thus represents a promising tool for both understanding metabolic regulation and developing novel therapies.
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