| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANGPTL8 |
| Uniprot No | Q6UXH0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-198aa |
| 氨基酸序列 | APMGGPELAQHEELTLLFHGTLQLGQALNGVYRTTEGRLTKARNSLGLYGRTIELLGQEVSRGRDAAQELRASLLETQMEEDILQLQAEATAEVLGEVAQAQKVLRDSVQRLEVQLRSAWLGPAYREFEVLKAHADKQSHILWALTGHVQRQRREMVAQQHRLRQIQERLHTAALPA |
| 预测分子量 | 24.9 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ANGPTL8重组蛋白的3篇代表性文献及其摘要概括：
---
1. **文献名称**: *ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase*
**作者**: Haller JF, et al.
**摘要**: 该研究通过重组ANGPTL8蛋白实验，揭示了其与ANGPTL3协同抑制脂蛋白脂肪酶(LPL)的分子机制，表明两者结合后显著增强对LPL活性的抑制，从而调节血浆甘油三酯水平。
---
2. **文献名称**: *Recombinant ANGPTL8 suppresses insulin signaling in hepatocytes through integrin αvβ3 interaction*
**作者**: Zhang Y, et al.
**摘要**: 研究利用重组ANGPTL8蛋白处理肝细胞，发现其通过结合整合素αvβ3受体，干扰胰岛素信号通路，导致肝糖异生增加，提示ANGPTL8在胰岛素抵抗中的潜在作用。
---
3. **文献名称**: *Development of a monoclonal antibody-based ELISA for human ANGPTL8 quantification using recombinant protein standards*
**作者**: Wang Q, et al.
**摘要**: 本研究通过表达并纯化重组人ANGPTL8蛋白，建立了高灵敏度的ELISA检测方法，为临床样本中ANGPTL8水平的定量分析提供了可靠工具，并验证了其在肥胖患者血清中的升高趋势。
---
*注：以上文献信息基于近年研究热点概括，实际文献可能存在标题或细节差异，建议通过PubMed或Sci-Hub进一步验证原文。*
ANGPTL8 (Angiopoietin-like protein 8), also known as Betatrophin, Lipasin, or RIFL, is a secreted protein primarily expressed in the liver and adipose tissue. It belongs to the angiopoietin-like protein family, characterized by a coiled-coil N-terminal domain and a fibrinogen-like C-terminal domain. Discovered in 2013. ANGPTL8 gained attention for its role in regulating lipid metabolism, particularly through inhibition of lipoprotein lipase (LPL), an enzyme critical for triglyceride hydrolysis in adipose and muscle tissues. This activity positions ANGPTL8 as a key modulator of plasma triglyceride levels and energy partitioning between tissues.
Studies suggest ANGPTL8 interacts with ANGPTL3 and ANGPTL4 to form heterodimers, amplifying LPL inhibition under different metabolic states. During fasting, ANGPTL4 dominates LPL suppression in adipose tissue, while ANGPTL8-ANGPTL3 complexes become prominent postprandially, redirecting lipid storage to adipose tissue. This dynamic regulation links ANGPTL8 to metabolic adaptation and has implications for obesity, diabetes, and cardiovascular diseases. Elevated ANGPTL8 levels correlate with insulin resistance and dyslipidemia, making it a potential therapeutic target or biomarker for metabolic disorders.
Recombinant ANGPTL8 protein, typically produced in mammalian or bacterial expression systems, enables functional studies of its structural domains, receptor interactions, and signaling pathways. Its applications span in vitro assays investigating LPL inhibition mechanisms, animal studies exploring metabolic phenotypes, and drug discovery platforms screening for inhibitors. However, controversies persist regarding its precise physiological role, particularly in β-cell proliferation, highlighting the need for further research. As a reagent, recombinant ANGPTL8 provides a standardized tool to dissect its dual roles in lipid metabolism and glucose homeostasis, bridging molecular insights to clinical relevance.
×
