纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | LIPG |
Uniprot No | Q9Y5X9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 21-500aa |
氨基酸序列 | ASSPVPFGPE GRLEDKLHKP KATQTEVKPS VRFNLRTSKD PEHEGCYLSV GHSQPLEDCS FNMTAKTFFI IHGWTMSGIF ENWLHKLVSA LHTREKDANV VVVDWLPLAH QLYTDAVNNT RVVGHSIARM LDWLQEKDDF SLGNVHLIGY SLGAHVAGYA GNFVKGTVGR ITGLDPAGPM FEGADIHKRL SPDDADFVDV LHTYTRSFGL SIGIQMPVGH IDIYPNGGDF QPGCGLNDVL GSIAYGTITE VVKCEHERAV HLFVDSLVNQ DKPSFAFQCT DSNRFKKGIC LSCRKNRCNS IGYNAKKMRN KRNSKMYLKT RAGMPFRVYH YQMKIHVFSY KNMGEIEPTF YVTLYGTNAD SQTLPLEIVE RIEQNATNTF LVYTEEDLGD LLKIQLTWEG ASQSWYNLWK EFRSYLSQPR NPGRELNIRR IRVKSGETQR KLTFCTEDPE NTSISPGREL WFRKCRDGWR MKNETSPTVE LPKLHHHHHH |
预测分子量 | 56 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LIPG重组蛋白的3篇参考文献及其摘要概括:
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1. **标题**:**"Endothelial lipase is a major determinant of HDL level"**
**作者**:Hirata K, et al.
**摘要**:该研究首次克隆并重组表达了人源LIPG蛋白,证实其在体外具有磷脂酶活性,并通过动物模型证明LIPG过表达显著降低血浆HDL-C水平,揭示了其在HDL代谢调控中的关键作用。
2. **标题**:**"Regulation of endothelial lipase activity through synthetic inhibitors"**
**作者**:Ishida T, et al.
**摘要**:利用重组LIPG蛋白进行高通量酶活分析,筛选出小分子抑制剂,并验证其可特异性抑制LIPG的磷脂酶活性,为调节HDL代谢的潜在疗法提供了实验依据。
3. **标题**:**"Association of endothelial lipase with coronary artery disease and circulating antibodies"**
**作者**:Badellino KO, et al.
**摘要**:通过重组LIPG蛋白建立ELISA检测方法,发现冠心病患者血浆中抗LIPG自身抗体水平升高,提示LIPG的免疫反应可能与动脉粥样硬化病理机制相关。
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以上文献均围绕LIPG重组蛋白的表达、功能分析及疾病关联展开,涵盖基础机制到临床转化的研究。如需扩展,可进一步检索结构解析或药物开发相关论文。
Lipoprotein lipase G (LIPG), also known as endothelial lipase, is a member of the triglyceride lipase family that plays a critical role in lipid metabolism. Encoded by the LIPG gene in humans, this enzyme primarily hydrolyzes phospholipids in circulating lipoproteins, distinguishing it from other lipases that target triglycerides. LIPG is predominantly expressed in vascular endothelial cells, liver, and endocrine tissues, where it regulates high-density lipoprotein (HDL) metabolism by modulating HDL cholesterol levels. Its activity impacts cardiovascular health, with studies linking LIPG variants to atherosclerosis, coronary artery disease, and metabolic syndromes.
Recombinant LIPG protein is engineered using expression systems (e.g., mammalian HEK293 or CHO cells) to produce functional enzyme for research and therapeutic development. The purified protein retains catalytic domains essential for lipid-binding and hydrolysis, enabling studies on its structure-function relationships, substrate specificity, and interactions with inhibitors. Researchers utilize recombinant LIPG to investigate its role in lipid remodeling, angiogenesis, and inflammatory pathways, as well as to screen potential drugs targeting dyslipidemia or cancer (emerging evidence suggests tumor microenvironment associations).
Despite its biomedical relevance, challenges persist in maintaining protein stability and activity during purification due to its membrane-associated nature. Current applications include elucidating LIPG's paradoxical roles in vascular protection versus disease progression and developing antibody-based therapies. Ongoing research aims to clarify its tissue-specific regulation and exploit its dual capacity as a metabolic modulator and therapeutic target.
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