| Cat# | DIA-282 |
| Source | Pseudomonas species |
| Description | Enzyme that hydrolyzes triglycerides into three free fatty acids and glycerol. Take advantage of the enhanced liquid stability of this enzyme. Rely on the proven diagnostic quality of this product. |
| Activity | >10 U/mg lyophilizate |
| Synonyms | Lipoprotein lipase; LPL; Clearing factor lipase; Diacylglycerol lipase; Diglyceride lipase |
| pH Stability | 6.0-10.0 |
| Optimum pH | 7.5 |
| Thermal stability | Up to +50°C |
| Stability | At +2 to +8°C within specification range for 12 months. Store dry. |
| Contaminants | ATPase: <0.005 Catalase: <1.0 Glycerokinase: <0.001 Hexokinase: <0.005 ''NADH oxidase'': <0.001 Uricase: <0.005 |
| Abbr | Chemically modified LPL (Pseudomonas sp.) |
| Alias | LPL |
| Applications | Use Lipoprotein lipase in diagnostic tests for the determination of triglycerides together with Glycerol Kinase and Glycerol-3-phosphate Dehydrogenase. |
| Appearance | Brownish lyophilizate |
| Molecular Weight | 47 kD |
| Specificity | Lipoprotein Lipase has both lipolytic and sterol ester hydrolytic activities. It hydrolyzes triacylglycerols in chylomicrons, lipoproteins and diacylglycerols. With human plasma as substrate triglycerides are hydrolyzed more rapidly than cholesterol esters. The effects of pH and ionic strength on the enzymatic activity are somewhat different between the hydrolysis of triglyceride and of cholesterol ester depending on the different states of these substrates in the plasma or the transfer of the reaction products at the interface of substrates. |
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