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| 纯度 | >= 95 % HPLC. |
| 种属 | Human |
| 靶点 | Acrp30 |
| Uniprot No | Q15848 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-244aa |
| 氨基酸序列 | ETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEK GDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVG LETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYM KDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGE GERNGLYADNDNDSTFTGFLLYHDTN |
| 预测分子量 | 25 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Acrp30(脂联素)重组蛋白的3篇经典文献及其摘要概括：
1. **文献名称**：*A novel serum protein similar to C1q, produced exclusively in adipocytes*
**作者**：Scherer, P.E. 等(1995)
**摘要**：首次从小鼠脂肪细胞中克隆并鉴定了Acrp30(脂联素)，描述了其与补体C1q的结构相似性，并证明其通过重组蛋白形式在哺乳动物细胞中表达，为后续研究其代谢调节功能奠定基础。
2. **文献名称**：*The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity*
**作者**：Yamauchi, T. 等(2001)
**摘要**：研究利用重组Acrp30蛋白治疗胰岛素抵抗模型小鼠，发现其能显著改善糖代谢异常，降低血糖和血脂水平，揭示了其在肥胖和脂肪萎缩相关代谢疾病中的潜在治疗价值。
3. **文献名称**：*Cloning of adiponectin receptors that mediate antidiabetic metabolic effects*
**作者**：Yamauchi, T. 等(2003)
**摘要**：通过重组Acrp30蛋白筛选，鉴定了脂联素受体AdipoR1和AdipoR2.证实其介导了脂联素激活AMPK和PPAR-α信号通路的机制，为阐明脂联素改善胰岛素敏感性的分子机制提供关键证据。
4. **文献名称**：*Structure-function studies of the adipocyte-secreted hormone Acrp30/adiponectin*
**作者**：Berg, A.H. 等(2002)
**摘要**：分析了重组Acrp30蛋白的多聚体结构(低分子量、中分子量和高分子量形式)，发现高分子量形式在调节胰岛素敏感性和脂肪酸氧化中起主要作用，强调了结构对其生理功能的重要性。
(注：若需具体文献来源或补充PMID/DOI，可进一步提供。)
Acrp30. also known as adiponectin, is a protein hormone predominantly secreted by adipose tissue, playing a critical role in regulating glucose metabolism, fatty acid oxidation, and insulin sensitivity. Discovered in the mid-1990s, it gained attention for its paradoxical association with obesity; circulating levels inversely correlate with body fat mass, suggesting a compensatory mechanism to counteract metabolic dysfunction. Structurally, Acrp30 exists in multiple oligomeric forms—trimers, hexamers, and high-molecular-weight multimers—each with distinct biological activities. Its receptors, AdipoR1 and AdipoR2. are widely expressed in tissues like liver, muscle, and brain, mediating metabolic effects through AMPK and PPAR-α signaling pathways.
Recombinant Acrp30 is produced via genetic engineering, often using bacterial or mammalian expression systems, to study its therapeutic potential. Preclinical studies highlight its anti-inflammatory, anti-atherogenic, and insulin-sensitizing properties, making it a candidate for treating metabolic disorders such as type 2 diabetes, obesity, and non-alcoholic fatty liver disease. Notably, its ability to enhance mitochondrial biogenesis and reduce gluconeogenesis has spurred interest in drug development. However, challenges remain in stabilizing its high-molecular-weight forms and optimizing delivery methods for clinical use. Current research focuses on developing Acrp30 mimetics or receptor agonists to overcome these limitations, aiming to harness its metabolic benefits while circumventing the technical hurdles of protein-based therapies.
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