| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GHRL |
| Uniprot No | Q9UBU3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-51aa |
| 氨基酸序列 | GSSFLSPEHQRVQQRKESKKPPAKLQPR |
| 预测分子量 | 34.8 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GHRL(Ghrelin)重组蛋白的3篇参考文献示例(注：以下内容为模拟生成，实际文献请通过学术数据库查询)：
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1. **文献名称**: *Recombinant Ghrelin Improves Cardiac Function in Rats with Heart Failure*
**作者**: Smith A, et al.
**摘要**: 研究通过大肠杆菌表达系统成功制备重组Ghrelin蛋白，验证其促进生长激素释放的活性，并发现其通过激活AMPK通路改善心力衰竭模型大鼠的心肌功能。
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2. **文献名称**: *Expression and Purification of Bioactive Ghrelin in Yeast*
**作者**: Chen L, Wang Y.
**摘要**: 报道利用毕赤酵母系统高效表达人源Ghrelin，通过亲和层析纯化获得高纯度蛋白，体外实验证实其可显著增强食欲相关神经元活性。
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3. **文献名称**: *Therapeutic Potential of Recombinant Ghrelin in Cancer Cachexia*
**作者**: Tanaka K, et al.
**摘要**: 在小鼠肿瘤模型中，注射重组Ghrelin蛋白有效逆转肌肉萎缩和体重下降，机制涉及抑制促炎因子IL-6及激活GHRL/GHSR信号通路。
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(提示：实际研究中建议通过PubMed或Web of Science以关键词"recombinant ghrelin/protein" + "expression/therapy/function"检索最新文献。)
**Background of GHRL Recombinant Protein**
Ghrelin (GHRL), a 28-amino-acid peptide hormone, was first identified in 1999 as an endogenous ligand for the growth hormone secretagogue receptor (GHSR). Primarily synthesized in the stomach, ghrelin plays a pivotal role in regulating appetite, energy balance, and glucose metabolism. Its unique post-translational modification—octanoylation at serine 3—is essential for binding to GHSR-1a, thereby activating signaling pathways that stimulate hunger and growth hormone release.
Recombinant GHRL protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to mimic the native peptide’s structure and function. Advanced purification techniques ensure high purity and bioactivity, critical for research and therapeutic applications. Unlike animal-derived ghrelin, recombinant variants offer scalability, consistency, and reduced immunogenicity, making them ideal for standardized studies.
GHRL recombinant protein is widely used in metabolic research, particularly in obesity, diabetes, and cachexia studies. It serves as a tool to explore mechanisms linking gut-brain signaling to feeding behavior, insulin sensitivity, and energy homeostasis. Clinically, it holds potential for treating conditions like anorexia or muscle-wasting syndromes, though challenges related to its short half-life and stability *in vivo* persist. Recent innovations, including acylated analogs and delivery systems, aim to enhance its therapeutic efficacy.
Overall, GHRL recombinant protein bridges basic science and translational medicine, offering insights into metabolic regulation and paving the way for novel interventions in metabolic disorders.
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