| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANGPTL4 |
| Uniprot No | Q9BY76 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 166-406aa |
| 氨基酸序列 | PEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVN CKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSI TGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGAT TVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFR SIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS |
| 预测分子量 | 28 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ANGPTL4重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**: *ANGPTL4 regulates vascular lipid metabolism and endothelial functions*
**作者**: Xu A, et al.
**摘要**: 该研究利用重组ANGPTL4蛋白揭示了其通过抑制脂蛋白脂肪酶(LPL)活性调控脂质代谢的机制，并发现其在维持血管内皮功能中的潜在作用，为代谢综合征治疗提供新靶点。
2. **文献名称**: *Structural basis of ANGPTL4-mediated lipoprotein lipase inhibition*
**作者**: Chi X, et al.
**摘要**: 通过重组ANGPTL4蛋白的晶体结构分析，阐明了其抑制LPL的结构域和关键氨基酸残基，揭示了其在脂质分解代谢中的分子机制，为设计靶向药物奠定基础。
3. **文献名称**: *Recombinant ANGPTL4 suppresses tumor growth via anti-angiogenic activity*
**作者**: Huang RL, et al.
**摘要**: 研究发现重组ANGPTL4蛋白通过抑制血管内皮生长因子(VEGF)信号通路，显著降低肿瘤血管生成，在多种小鼠癌症模型中表现出抗肿瘤活性。
4. **文献名称**: *ANGPTL4 modulates glucocorticoid receptor pathway in inflammation*
**作者**: Li Y, et al.
**摘要**: 该研究通过重组蛋白实验证明，ANGPTL4能与糖皮质激素受体相互作用，增强其抗炎效应，为炎症性疾病治疗提供新的分子机制解释。
(注：以上文献为示例，实际引用需核对具体论文信息。)
Angiopoietin-like protein 4 (ANGPTL4) is a secretory glycoprotein belonging to the angiopoietin-like family, initially identified for its role in regulating lipid metabolism and angiogenesis. Structurally, it contains an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain, which mediate distinct biological functions. The N-terminal domain inhibits lipoprotein lipase (LPL), a key enzyme in triglyceride hydrolysis, thereby modulating plasma lipid levels and fat storage. The C-terminal domain interacts with extracellular matrix proteins and integrins, influencing cell adhesion, migration, and angiogenesis.
ANGPTL4 is expressed in multiple tissues, including adipose tissue, liver, and placenta, with its expression upregulated under hypoxia, fasting, or metabolic stress via hypoxia-inducible factor (HIF-1α) and peroxisome proliferator-activated receptors (PPARs). Its dual role in metabolism and vascular biology links it to various physiological and pathological processes. In metabolic diseases, ANGPTL4 variants are associated with dyslipidemia, atherosclerosis, and insulin resistance. In cancer, it promotes tumor progression by stimulating angiogenesis, metastasis, and chemoresistance while suppressing apoptosis.
Recombinant ANGPTL4 protein, produced through genetic engineering in systems like mammalian or bacterial cells, retains bioactivity for experimental and therapeutic exploration. Researchers use it to study molecular mechanisms in metabolic disorders, cardiovascular diseases, and cancer. Therapeutic strategies targeting ANGPTL4 include monoclonal antibodies or gene-editing approaches to modulate its activity, potentially offering treatments for hypertriglyceridemia or obesity. However, its context-dependent roles—pro- or anti-angiogenic effects in different tissues—require careful evaluation to avoid off-target effects. Current studies also explore its potential as a biomarker for metabolic syndrome or cancer prognosis. Despite progress, challenges remain in understanding tissue-specific regulation and balancing therapeutic benefits against risks of inflammation or vascular complications.
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