人 Lipoprotein Lipase 抗体对
01AB00873
Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism, responsible for hydrolyzing triglycerides in circulating lipoproteins, such as chylomicrons and very low-density lipoproteins (VLDL), into free fatty acids and monoacylglycerol. This process provides energy substrates for tissues like adipose, skeletal muscle, and the heart. LPL functions as a non-covalent homodimer and requires ApoC-II as a cofactor for activation. It is anchored to the endothelial surface via glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1). Structurally, LPL contains an N-terminal α/β hydrolase domain with a catalytic triad (Ser159, Asp183, His268) and a C-terminal β-barrel domain that determines substrate specificity. These domains are connected by a hinge region critical for enzymatic activity. Mutations or deficiencies in LPL can lead to familial chylomicronemia syndrome (FCS), characterized by severe hypertriglyceridemia, pancreatitis, and lipid deposition disorders. Dysregulated LPL activity has also been implicated in obesity, diabetes, and cardiovascular diseases.
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技术参数
- 靶点基因名
- LPL
- 基因别名
- LIPD
- 蛋白别名
- lipoprotein lipase; Lipoprotein Lipase
- UniProt
- P06858
- 物种
- Human
产品详情
- 靶点名称
- Lipoprotein Lipase
- 蛋白名称
- lipoprotein lipase
- 蛋白别名
- Lipoprotein lipase; LPL; Phospholipase A1
- 靶点基因名
- LPL
- 基因别名
- LIPD
- UniProt
- P06858
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism, responsible for hydrolyzing triglycerides in circulating lipoproteins, such as chylomicrons and very low-density lipoproteins (VLDL), into free fatty acids and monoacylglycerol. This process provides energy substrates for tissues like adipose, skeletal muscle, and the heart. LPL functions as a non-covalent homodimer and requires ApoC-II as a cofactor for activation. It is anchored to the endothelial surface via glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1). Structurally, LPL contains an N-terminal α/β hydrolase domain with a catalytic triad (Ser159, Asp183, His268) and a C-terminal β-barrel domain that determines substrate specificity. These domains are connected by a hinge region critical for enzymatic activity. Mutations or deficiencies in LPL can lead to familial chylomicronemia syndrome (FCS), characterized by severe hypertriglyceridemia, pancreatitis, and lipid deposition disorders. Dysregulated LPL activity has also been implicated in obesity, diabetes, and cardiovascular diseases.