| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APLN |
| Uniprot No | Q9ULZ1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-77aa |
| 氨基酸序列 | LVQPRGSRN GPGPWQGGRR KFRRQRPRLS HKGPMPF |
| 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APLN(Apelin)重组蛋白的3篇代表性文献信息及摘要概括：
1. **文献名称**：*Recombinant Apelin Improves Cardiac Function in Rats with Heart Failure by Activating the APJ/Akt Signaling Pathway*
**作者**：Zhang Y, et al.
**摘要**：研究团队通过原核表达系统制备重组Apelin蛋白，验证其在心力衰竭大鼠模型中的治疗潜力。实验表明，重组Apelin通过激活APJ受体及下游Akt通路，显著增强心肌收缩力并抑制纤维化，提示其作为心衰治疗药物的潜力。
2. **文献名称**：*Expression and Purification of Functional Human Apelin-13 in Escherichia coli for Angiogenesis Studies*
**作者**：Li X, et al.
**摘要**：该文献报道了一种高效的大肠杆菌表达体系生产具有生物活性的重组人Apelin-13.纯化后的蛋白在体外实验中被证实可促进内皮细胞增殖和血管生成，为研究Apelin在缺血性疾病中的作用提供了可靠工具。
3. **文献名称**：*Role of Recombinant Apelin in Alleviating Insulin Resistance in Type 2 Diabetic Mice*
**作者**：Wang L, et al.
**摘要**：通过酵母表达系统制备重组Apelin，并在2型糖尿病小鼠模型中验证其代谢调节功能。结果显示，重组Apelin能显著改善胰岛素敏感性、降低血糖水平，机制涉及AMPK信号通路的激活。
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**备注**：以上文献信息为示例性质，实际引用时需根据具体研究需求检索PubMed或Web of Science获取原文。建议优先选择近5年发表、影响因子较高的期刊论文，并关注重组蛋白的生产技术(如原核/真核表达系统优化)或疾病治疗应用方向的研究。
**Background of APLN Recombinant Protein**
APLN (apelin) is a bioactive peptide encoded by the *APLN* gene, functioning as an endogenous ligand for the G protein-coupled receptor APJ (APLNR). Discovered in 1998. apelin is involved in diverse physiological processes, including cardiovascular regulation, fluid homeostasis, metabolic balance, and angiogenesis. It exists in multiple isoforms, such as apelin-36. apelin-17. and apelin-13. derived from proteolytic cleavage of a preproprotein. The shortest active form, apelin-13. exhibits high receptor-binding affinity and biological activity.
Recombinant APLN protein is engineered using biotechnological methods, often expressed in *E. coli*, yeast, or mammalian cell systems to ensure proper folding and post-translational modifications. Its production enables large-scale studies on apelin's role in diseases like heart failure, hypertension, diabetes, and cancer. Apelin/APJ signaling promotes vasodilation, cardiomyocyte contractility, and angiogenesis while suppressing inflammation and oxidative stress, making it a therapeutic target. In metabolic disorders, apelin modulates insulin sensitivity and adipocyte function, highlighting its potential in obesity-related therapies.
Research utilizing APLN recombinant protein has advanced drug development, including peptide analogs and receptor modulators. However, its dual role in pathologies (e.g., pro-angiogenic effects in tumors) necessitates careful therapeutic targeting. As a tool compound, recombinant APLN aids in elucidating molecular mechanisms and screening therapeutic candidates, bridging translational gaps in cardiovascular and metabolic research.
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