Native Burkholderia sp. Lipoprotein Lipase
Native Burkholderia sp. Lipoprotein Lipase

Native Burkholderia sp. Lipoprotein Lipase

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.
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