| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPIHBP1 |
| Uniprot No | Q8IV16 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MKALGAVLLA LLLCGRPGRG QTQQEEEEED EDHGPDDYDE EDEDEVEEEE TNRLPGGRSR VLLRCYTCK SLPRDERCNL TQNCSHGQTC TTLIAHGNTE SGLLTTHSTW CTDSCQPITK TVEGTQVTM TCCQSSLCNV PPWQSSRVQD PTGKGAGGPR GS |
| 预测分子量 | 17 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GPIHBP1重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *GPIHBP1. a novel endothelial cell transporter for lipoprotein lipase*
**作者**: Beigneux AP, et al.
**摘要**: 本文首次发现GPIHBP1是毛细血管内皮细胞表面结合并转运脂蛋白脂肪酶(LPL)的关键蛋白。研究通过重组GPIHBP1蛋白实验证明其能与LPL特异性结合，并揭示了其在脂质代谢中的核心作用。
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2. **文献名称**: *Lipoprotein lipase and its regulator GPIHBP1: Structure, function, and interactions*
**作者**: Weinstein MM, et al.
**摘要**: 通过重组GPIHBP1与LPL的体外结合实验，阐明了二者相互作用的结构基础。研究发现GPIHBP1不仅能稳定LPL活性，还能介导乳糜微粒与内皮细胞的结合，为高甘油三酯血症的机制提供了新见解。
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3. **文献名称**: *GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by ANGPTL3/4/8*
**作者**: Chi X, et al.
**摘要**: 该研究利用重组GPIHBP1蛋白证明其通过结合LPL并屏蔽ANGPTL家族蛋白(如ANGPTL3/4/8)的抑制效应，维持LPL酶活性。动物模型中，重组GPIHBP1可显著恢复LPL缺陷小鼠的血脂水平。
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**备注**：以上文献均聚焦于GPIHBP1重组蛋白在LPL功能调控、脂代谢疾病模型中的应用及分子机制。如需具体发表年份或期刊，建议通过PubMed或Google Scholar检索标题进一步验证。
GPIHBP1 (glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1) is a cell-surface protein predominantly expressed in capillary endothelial cells, particularly in tissues with high lipid metabolism like heart, muscle, and adipose. Discovered in 2007. it plays a critical role in lipid transport by anchoring lipoprotein lipase (LPL) to the capillary lumen, enabling the hydrolysis of triglyceride-rich lipoproteins (e.g., chylomicrons, VLDL) into free fatty acids for energy production or storage. Structurally, GPIHBP1 contains an N-terminal acidic domain that binds LPL and a cysteine-rich LU domain that stabilizes LPL activity. Its GPI anchor tethers the protein to endothelial cells while allowing lateral mobility.
Mutations in *GPIHBP1* are linked to severe hypertriglyceridemia (e.g., familial chylomicronemia syndrome), characterized by impaired LPL function, elevated plasma triglycerides, and pancreatitis risk. This established GPIHBP1 as a key regulator of plasma triglyceride homeostasis. Recombinant GPIHBP1 proteins, typically produced in mammalian expression systems (e.g., CHO cells), retain functional domains for LPL binding and stabilization. These proteins are used to study LPL-GPIHBP1 interactions, model lipid disorders, and develop therapeutic strategies. Recent research explores recombinant GPIHBP1 as a potential treatment for LPL-related diseases or as a tool to enhance LPL delivery in gene therapies. Its ability to "rescue" dysfunctional LPL in vitro underscores its therapeutic relevance. Additionally, recombinant GPIHBP1 serves in diagnostic assays to detect autoantibodies in rare autoimmune hypertriglyceridemia cases. Ongoing studies focus on its structural biology and tissue-specific regulatory mechanisms to refine targeted interventions.
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