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纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | apM1 |
Uniprot No | Q60994 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 18-247aa |
氨基酸序列 | EDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN |
预测分子量 | 28.9 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apM1(脂联素)重组蛋白的3篇参考文献示例:
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1. **文献名称**: *Production of recombinant human adiponectin (apM1) in Escherichia coli and its biological activity*
**作者**: Waki, H. 等
**摘要**: 研究成功利用大肠杆菌表达系统制备重组人脂联素,验证其通过激活AMPK通路促进脂肪酸氧化和葡萄糖摄取的能力,为代谢疾病研究提供工具。
2. **文献名称**: *Crystal structure of globular adiponectin (apM1) and its receptor interaction mechanism*
**作者**: Shapiro, L. 等
**摘要**: 解析了脂联素球状结构域的晶体结构,揭示了其与受体结合的新型结构基序,为靶向药物设计提供结构基础。
3. **文献名称**: *Therapeutic effects of recombinant adiponectin (apM1) on diabetic mice with insulin resistance*
**作者**: Yamauchi, T. 等
**摘要**: 在2型糖尿病模型小鼠中,重组脂联素显著改善胰岛素敏感性并降低炎症因子水平,证实其潜在治疗代谢综合征的作用。
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*注:以上文献为示例性质,具体作者与内容需根据实际检索结果调整。建议通过PubMed或Google Scholar以关键词“recombinant adiponectin/apM1”获取准确文献。*
apM1 recombinant protein, also known as adiponectin, is a hormone predominantly secreted by adipose tissue that plays a critical role in metabolic regulation. Encoded by the APM1 (Adipose Most Abundant Gene Transcript 1) gene, this 30-kDa protein consists of 244 amino acids and structurally includes a collagen-like domain and a globular C-terminal domain. Adiponectin exists in multiple oligomeric forms (trimers, hexamers, and high-molecular-weight complexes), each with distinct biological activities. It enhances insulin sensitivity, promotes glucose uptake in skeletal muscle, and suppresses hepatic glucose production, making it a key modulator of energy homeostasis.
Research has linked low adiponectin levels to obesity, type 2 diabetes, and cardiovascular diseases, positioning it as a biomarker and therapeutic target. Recombinant apM1 protein is produced using expression systems like *E. coli* or mammalian cells, followed by purification via affinity chromatography. Its production enables functional studies on adiponectin signaling pathways, particularly interactions with AdipoR1 and AdipoR2 receptors, which activate AMPK and PPAR-α pathways to regulate lipid metabolism and anti-inflammatory responses.
Preclinical studies demonstrate that recombinant adiponectin improves insulin resistance, reduces atherosclerosis, and mitigates inflammation in animal models. However, challenges remain in stabilizing its high-molecular-weight isoforms and optimizing delivery methods for clinical use. Current applications span basic research, drug discovery, and exploration of adiponectin-based therapies for metabolic disorders. Structural analyses of recombinant apM1 also aid in designing mimetic peptides or small molecules to replicate its therapeutic effects. This protein continues to be a focal point in understanding the interplay between adipose tissue dysfunction and systemic metabolism.
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