| Cat# | NATE-0417 |
| Source | Burkholderia sp. |
| Description | Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. LPL is attached to the luminal surface of endothelial cells in capillaries by the protein glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1) and by heparin sulfated proteoglycans. It is most widely distributed in adipose, heart, and skeletal muscle tissue, as well as in lactating mammary glands. |
| Form | lyophilized powder |
| Activity | > 50,000 units/mg solid |
| CAS No. | 9004-02-8 |
| Unit Definition | One unit will release 1.0 nmole of p-nitrophenol per min at pH 7.2 at 37°C using p-nitrophenyl butyrate as substrate. |
| Storage | ?20°C |
| Synonyms | lipoprotein lipase; clearing factor lipase; diglyceride lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor; EC 3.1.1.34; 9004-02-8; LPL |
| Enzyme Commission Number | EC 3.1.1.34 |
| Abbr | LPL, Native (Burkholderia sp.) |
| Alias | LPL |
| Applications | Lipoprotein lipase has been used in a study to assess the role of lipogenic enzymes in colorectal cancer. It has also been used in a study to investigate lipasemic activity of low molecular weight heparin in rats. |
| Product Overview | Lipoprotein lipase hydrolyzes triglycerides in plasma lipoproteins causing release of fatty acids for metabolic purposes in muscles and adipose tissue. |
| Download Datasheet: |  |
