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.
Abbr
LPL, Native (Bovine)
Form
ammonium sulfate suspension; Suspension in 3.8 M ammonium sulfate, 0.02 M Tris HCl, pH 8.0
Enzyme Commission Number
EC 3.1.1.34
Activity
> 2,000 units/mg protein (BCA)
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.
Warnings
Affinity purified
Pathway
Adipogenesis, organism-specific biosystem; Chylomicron-mediated lipid transport, organism-specific biosystem; Glycerolipid metabolism, conserved biosystem
Function
apolipoprotein binding; lipoprotein lipase activity; protein binding
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
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