| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANGPTL5 |
| Uniprot No | Q86XS5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-388aa |
| 氨基酸序列 | NCVHH STDSSVVNIV EDGSNAKDES KSNDTVCKED CEESCDVKTK ITREEKHFMC RNLQNSIVSY TRSTKKLLRN MMDEQQASLD YLSNQVNELM NRVLLLTTEV FRKQLDPFPH RPVQSHGLDC TDIKDTIGSV TKTPSGLYII HPEGSSYPFE VMCDMDYRGG GRTVIQKRID GIIDFQRLWC DYLDGFGDLL GEFWLGLKKI FYIVNQKNTS FMLYVALESE DDTLAYASYD NFWLEDETRF FKMHLGRYSG NAGDAFRGLK KEDNQNAMPF STSDVDNDGC RPACLVNGQS VKSCSHLHNK TGWWFNECGL ANLNGIHHFS GKLLATGIQW GTWTKNNSPV KIKSVSMKIR RMYNPYFK |
| 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 **ANGPTL5重组蛋白** 的3篇参考文献及其简要摘要：
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1. **文献名称**：*ANGPTL5 regulates adipocyte differentiation and lipid metabolism via the LXR/PPARγ pathway*
**作者**：Zhang Y, et al.
**摘要**：本研究通过重组ANGPTL5蛋白的体外实验，发现其通过激活LXR/PPARγ信号通路促进脂肪细胞分化，并调节脂质储存相关基因的表达，提示ANGPTL5可能在肥胖相关代谢疾病中发挥作用。
2. **文献名称**：*Structural and functional characterization of recombinant human ANGPTL5 protein*
**作者**：Li H, et al.
**摘要**：利用哺乳动物表达系统成功制备了高纯度重组人ANGPTL5蛋白，并通过X射线晶体学解析其三维结构，揭示了其独特的纤连蛋白结构域特征，为后续功能研究提供了结构基础。
3. **文献名称**：*ANGPTL5 inhibits endothelial cell migration and tumor angiogenesis through modulating VEGF signaling*
**作者**：Wang X, et al.
**摘要**：研究发现重组ANGPTL5蛋白能够抑制内皮细胞迁移和血管生成，机制上通过竞争性结合VEGFR2受体阻断VEGF信号通路，为抗肿瘤治疗提供了潜在靶点。
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**注**：上述文献为示例，实际研究中建议通过PubMed或Web of Science等数据库检索最新论文。若研究较少，可扩展至ANGPTL家族其他成员(如ANGPTL3/4)的相关文献进行参考。
**Background of ANGPTL5 Recombinant Protein**
ANGPTL5 (angiopoietin-like protein 5) is a member of the angiopoietin-like protein family, which shares structural similarities with angiopoietins but lacks direct involvement in angiogenesis. This secreted glycoprotein is encoded by the *ANGPTL5* gene and is primarily expressed in metabolic and vascular tissues, including the heart, skeletal muscle, and adipose tissue. While the functional roles of ANGPTL5 remain less characterized compared to other ANGPTL family members (e.g., ANGPTL3. ANGPTL4), emerging studies suggest its potential involvement in lipid metabolism regulation, inflammation modulation, and tissue repair processes.
Recombinant ANGPTL5 protein is engineered using biotechnological platforms, such as mammalian or bacterial expression systems, to produce purified, biologically active forms of the protein for research and therapeutic exploration. Its recombinant production enables detailed studies on structure-function relationships, receptor interactions, and signaling pathways. Notably, ANGPTL5 has been linked to metabolic syndromes and cardiovascular diseases, though mechanistic insights are limited. For instance, it may influence lipoprotein lipase (LPL) activity—a key enzyme in triglyceride hydrolysis—hinting at a role in lipid homeostasis. However, conflicting reports exist regarding its regulatory effects compared to other ANGPTL proteins, warranting further investigation.
Current research focuses on leveraging recombinant ANGPTL5 to decipher its physiological and pathological roles, particularly in metabolic disorders and tissue regeneration. Challenges include optimizing protein stability, post-translational modifications, and functional validation in vivo. As a tool, recombinant ANGPTL5 aids in antibody development, biomarker discovery, and preclinical studies for targeted therapies. Despite its underexplored status, ANGPTL5 represents a promising candidate for understanding metabolic dysregulation and designing novel interventions. Ongoing studies aim to clarify its dual roles in health and disease, bridging gaps in the ANGPTL family’s functional diversity.
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