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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GH2 |
| Uniprot No | P01242 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-217aa |
| 氨基酸序列 | FPTI PLSRLFDNAM LRARRLYQLA YDTYQEFEEA YILKEQKYSF LQNPQTSLCF SESIPTPSNR VKTQQKSNLE LLRISLLLIQ SWLEPVQLLR SVFANSLVYG ASDSNVYRHL KDLEEGIQTL MWRLEDGSPR TGQIFNQSYS KFDTKSHNDD ALLKNYGLLY CFRKDMDKVE TFLRIVQCRS VEGSCGF |
| 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GH2重组蛋白的3篇示例参考文献(内容为模拟虚构，仅作格式参考)：
1. **文献名称**：*Expression and purification of recombinant GH2 in E. coli for structural studies*
**作者**：Smith J, et al.
**摘要**：本研究通过优化密码子和表达条件，在大肠杆菌中高效表达了GH2重组蛋白，并利用亲和层析技术纯化获得高纯度产物。通过圆二色谱分析证实其正确折叠，为后续结构解析奠定基础。
2. **文献名称**：*Functional characterization of GH2 recombinant protein in cellulose hydrolysis*
**作者**：Lee S, Zhang R.
**摘要**：首次报道GH2重组蛋白的纤维素酶活性，通过体外酶活实验证明其在pH 5.0、50℃条件下具有最佳催化效率。突变实验显示第132位谷氨酸为关键活性位点，为工业酶制剂开发提供依据。
3. **文献名称**：*Crystal structure analysis of GH2 from Bacillus subtilis*
**作者**：Wang X, et al.
**摘要**：采用X射线晶体学解析了枯草芽孢杆菌来源GH2蛋白的2.1Å分辨率三维结构，揭示其独特的(β/α)8桶状催化结构域，并通过分子对接阐明了底物结合模式，为理性设计热稳定性突变体提供结构基础。
注：以上文献为示例，实际研究中建议通过PubMed/Google Scholar检索真实文献(可尝试关键词："recombinant GH2 protein"、"GH2 heterologous expression")。
**Background of GH2 Recombinant Protein**
GH2 recombinant protein is a genetically engineered form of growth hormone (GH), typically derived from the GH2 gene, which encodes a critical peptide hormone involved in growth regulation, metabolism, and cellular repair. Native GH is primarily produced by the pituitary gland and plays a pivotal role in postnatal growth, tissue maintenance, and metabolic functions. The development of recombinant GH2 emerged to address limitations associated with early GH therapies, which relied on extraction from human or animal sources, posing risks of contamination and ethical concerns.
Recombinant GH2 is produced using recombinant DNA technology, where the GH2 gene is inserted into host systems like *E. coli*, yeast, or mammalian cell lines. These systems enable large-scale production of bioactive GH2 with high purity and consistency. The protein shares structural and functional homology with natural human GH, binding to GH receptors to activate signaling pathways such as JAK2-STAT, MAPK, and PI3K-AKT, which regulate cell proliferation, differentiation, and nutrient metabolism.
Therapeutic applications of GH2 recombinant protein include treating growth hormone deficiency (GHD) in children and adults, Turner syndrome, chronic kidney disease, and muscle-wasting conditions. It is also explored for anti-aging and athletic performance, though such uses remain controversial. Advantages over earlier therapies include reduced immunogenicity, batch-to-batch reliability, and scalability. Research continues to optimize delivery methods (e.g., sustained-release formulations) and expand clinical indications, balancing efficacy with safety profiles.
In summary, GH2 recombinant protein represents a cornerstone of modern biotechnology, merging molecular biology and medical science to address endocrine disorders and metabolic dysfunctions.
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