Overview
| 别名 | Lipoprotein lipase; LPL; Phospholipase A1 |
| 基因名 | Lipoprotein Lipase |
| UniProt ID | P06858 |
| 反应种属 | Human |
| 应用 | IHC-P |
| 宿主 | Mouse |
| 偶联物 | Unconjugated |
| 修饰 | Unmodified |
| 亚型 | IgG1 |
| 克隆号 | 4R8-L2-R2 |
| 克隆性 | Monoclonal Antibody |
| 分子量 | Calculated MW: 53 kDa |
| 纯化方式 | Affinity Purified |
| 产品形式 | Liquid |
| 推荐稀释比 | IHC-1:200-1:250 |
| 存储缓冲液 | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% sodium azide |
| 保存温度 | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| 背景信息 | 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. |
检测原理