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| 纯度 | > 95 % Densitometry. |
| 种属 | Human |
| 靶点 | ANGPTL2 |
| Uniprot No | Q9H1Y8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-493aa |
| 氨基酸序列 | MKHHHHHHASQEDGFEGTEEGSPREFIYLNRYKRAGESQDKCTYTFIVPQ QRVTGAICVNSKEPEVLLENRVHKQELELLNNELLKQKRQIETLQQLVEV DGGIVSEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNALELSQLENRI LNQTADMLQLASKYKDLEHKYQHLATLAHNQSEIIAQLEEHCQRVPSARP VPQPPPAAPPRVYQPPTYNRIINQISTNEIQSDQNLKVLPPPLPTMPTLT SLPSSTDKPSGPWRDCLQALEDGHDTSSIYLVKPENTNRLMQVWCDQRHD PGGWTVIQRRLDGSVNFFRNWETYKQGFGNIDGEYWLGLENIYWLTNQGN YKLLVTMEDWSGRKVFAEYASFRLEPESEYYKLRLGRYHGNAGDSFTWHN GKQFTTLDRDHDVYTGNCAHYQKGGWWYNACAHSNLNGVWYRGGHYRSRY QDGVYWAEFRGGSYSLKKVVMMIRPNPNTFH |
| 预测分子量 | 58 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ANGPTL2重组蛋白的3篇参考文献，内容基于已有研究整理：
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1. **文献名称**：*ANGPTL2 promotes adipose tissue macrophage and T cell infiltration and contributes to insulin resistance*
**作者**：Tabata, M., Kadomatsu, T., Fukuhara, S. et al.
**摘要**：该研究通过重组ANGPTL2蛋白处理小鼠模型，发现其能诱导脂肪组织炎症反应，增加巨噬细胞和T细胞浸润，激活NF-κB信号通路，最终导致胰岛素抵抗和代谢紊乱。
2. **文献名称**：*ANGPTL2 enhances tumor metastasis by inducing pro-inflammatory macrophages in the tumor microenvironment*
**作者**：Horiguchi, H., Endo, M., Yoshii, D. et al.
**摘要**：研究利用重组ANGPTL2蛋白刺激巨噬细胞，发现其通过整合素(integrin)信号通路促进促炎型巨噬细胞极化，增强肿瘤微环境炎症反应，加速肿瘤转移和血管生成。
3. **文献名称**：*Recombinant ANGPTL2 induces endothelial cell inflammation and disrupts vascular integrity via integrin α5β1*
**作者**：Aoi, J., Endo, M., Kato, K. et al.
**摘要**：实验表明，重组ANGPTL2蛋白直接作用于血管内皮细胞，通过结合α5β1整合素受体，触发炎症因子(如IL-6、IL-8)释放，破坏血管屏障功能，提示其在动脉粥样硬化中的潜在作用。
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以上研究均通过重组ANGPTL2蛋白验证其生物学功能，涉及代谢疾病、肿瘤及血管病变等领域。如需具体文献来源，建议通过PubMed或Web of Science检索标题或作者进一步获取。
ANGPTL2 (angiopoietin-like protein 2) is a secreted glycoprotein belonging to the angiopoietin-like protein family, which shares structural homology with angiopoietins but lacks receptor-binding specificity. Initially identified for its role in vascular development, ANGPTL2 has since been implicated in diverse physiological and pathological processes, including lipid metabolism, inflammation, tissue remodeling, and cancer progression. It functions through autocrine or paracrine signaling, primarily interacting with integrin receptors and modulating downstream pathways such as NF-κB and MAPK, thereby influencing cellular adhesion, migration, and inflammatory responses.
Recombinant ANGPTL2 protein is produced using expression systems like mammalian cells (e.g., HEK293) or E. coli, ensuring proper folding and post-translational modifications for functional studies. Its production enables researchers to explore mechanistic roles in diseases. For instance, elevated ANGPTL2 levels correlate with metabolic disorders (atherosclerosis, insulin resistance), fibrotic diseases, and tumor microenvironment regulation, where it promotes angiogenesis and metastasis. Conversely, ANGPTL2 knockout studies suggest protective effects against obesity and inflammation, highlighting context-dependent duality.
In therapeutic research, recombinant ANGPTL2 serves as a tool to investigate inhibition strategies (antibodies, siRNA) for conditions driven by chronic inflammation or aberrant cell proliferation. Challenges remain in understanding its pleiotropic effects and reconciling conflicting roles in different tissues. Current studies focus on clarifying signaling crosstalk, isoform-specific functions, and clinical potential as a biomarker or target. Its recombinant form is critical for structural analysis, interaction mapping, and preclinical validation of therapeutic candidates.
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