Lipoprotein Lipase (LPL) is a glycerol ester hydrolase. Several bacteria that produce LPL, belongs to the genus Pseudomonas, Serratia and Mucor.
Lipoprotein lipase hydrolyzes triglycerides in plasma lipoproteins causing release of fatty acids for metabolic purposes in muscles and adipose tissue. 
Lipoprotein Lipase from Burkholderia sp. has been used in the subcellular fractionation of mussel Mytilus galloprovincialis to identify the biomolecule attached to cytosolic fraction of okodaic acid. It has also been used to test its effect on serum amyloid A induced granulocyte colony-stimulated factor (G-CSF) expression in response to bacterial lipoprotein.
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. 
10 mg in glass bottle
50 mg in poly bottle
Due to its lipolytic activity, lipoprotein lipase was shown to effectively block the spread of hepatitis C virus into healthy cells. 
Lipoprotein Lipase (LPL) hydrolysis triacylglycerol moieties in chylomicron and low density lipoproteins. LPL attaches lipoprotein to the vessel wall and facilitates their uptake. Abnormalities in LPL is associated with Alzheimer′s disease, atherosclerosis, obesity and chylomicronaemia.
Lipoprotein lipase belongs to the family of triglyceride lipases. It hydrolyses triglycerides in triglyceride-rich ApoB-containing lipoproteins.
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.