| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCG |
| Uniprot No | P01275 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 53-89aa |
| 氨基酸序列 | HSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIA |
| 预测分子量 | 6.4kDa |
| 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GCG(胰高血糖素样肽-1相关)重组蛋白的3篇模拟参考文献示例(基于常见研究方向整理)：
1. **文献名称**：高效表达GCG重组蛋白的大肠杆菌系统优化及功能验证
**作者**：Zhang L, et al.
**摘要**：本研究通过优化大肠杆菌表达系统(如密码子偏好性、诱导条件)，成功实现GCG重组蛋白的高效可溶性表达，并通过体外实验证实其与GLP-1受体的特异性结合能力，为糖尿病治疗药物开发提供基础。
2. **文献名称**：GCG/GLP-1双受体激动剂重组蛋白的构建及其代谢调控作用
**作者**：Finan B, et al.
**摘要**：通过基因工程构建同时靶向GCG和GLP-1受体的双功能重组蛋白，动物实验显示其显著改善肥胖小鼠的血糖水平和脂肪代谢，提示其在代谢综合征治疗中的潜力。
3. **文献名称**：重组GCG蛋白的晶体结构解析及其信号传导机制
**作者**：Yang D, et al.
**摘要**：利用X射线晶体学解析GCG重组蛋白的三维结构，揭示其与受体结合的分子机制，为设计更稳定的GCG类似物提供结构生物学依据。
---
注：以上文献为示例性内容，实际文献需通过PubMed、Google Scholar等平台检索关键词如“recombinant GLP-1/GCG protein”或“glucagon receptor agonist”获取。
**Background of GCG Recombinant Protein**
GCG recombinant protein refers to engineered versions of glucagon (GCG), a critical peptide hormone involved in glucose metabolism. Naturally produced by pancreatic α-cells, glucagon counteracts insulin by stimulating hepatic glucose production during fasting or hypoglycemia. Its role in maintaining blood sugar homeostasis has made it a therapeutic target for conditions like severe hypoglycemia. However, traditional glucagon extracted from animal or human sources faced limitations in stability, scalability, and immunogenicity, driving the development of recombinant DNA-based production.
Advances in biotechnology enabled the synthesis of GCG recombinant proteins using expression systems such as *E. coli*, yeast, or mammalian cell cultures. These systems allow precise control over protein structure, purity, and yield, addressing challenges associated with natural extraction. Recombinant glucagon retains the native 29-amino-acid sequence, ensuring biological activity while minimizing batch-to-batch variability.
Beyond treating acute hypoglycemia, GCG recombinant proteins have expanded into metabolic disorder research. Modified analogs with prolonged half-lives or enhanced stability (e.g., via PEGylation or amino acid substitution) are explored for diabetes management, obesity, and even neurodegenerative diseases, where glucagon’s role in energy regulation intersects with neuronal health. Additionally, dual- or triple-agonists targeting glucagon receptors alongside GLP-1 or GIP receptors are under investigation to synergistically improve glycemic control and weight loss.
The evolution of GCG recombinant proteins exemplifies the intersection of peptide engineering and metabolic therapeutics, offering tailored solutions for complex diseases while highlighting the potential of bioengineering to refine natural hormones into safer, more effective drugs. Ongoing research continues to optimize delivery methods (e.g., nasal sprays, stable liquid formulations) and explore novel applications in precision medicine.
×
