L2254
Lipoprotein Lipase from bovine milk
ammonium sulfate suspension, ≥2,000 units/mg protein (BCA)
Synonym(s):
LPL, Phospholipase A1, Diacylglycerol acylhydrolase, Diacylglycerol lipase
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About This Item
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biological source
bovine milk
Quality Level
form
ammonium sulfate suspension
specific activity
≥2,000 units/mg protein (BCA)
storage temp.
2-8°C
General description
Research area: Cell Signaling
Lipoprotein Lipase (LPL) from bovine milk is a glycoprotein. It exists as a homodimer and comprises two N-linked oligosaccharides. It is heat-labile.Lipoprotein lipase is an enzyme found on the surface of vascular endothelial cells, where it is anchored to capillary walls. It is mainly present in adipose tissue, heart, and muscle tissue. It is synthesized by extrahepatic tissues, particularly adipocytes, and the gene encoding the protein is situated on chromosome 8p22.
Lipoprotein Lipase (LPL) from bovine milk is a glycoprotein. It exists as a homodimer and comprises two N-linked oligosaccharides. It is heat-labile.Lipoprotein lipase is an enzyme found on the surface of vascular endothelial cells, where it is anchored to capillary walls. It is mainly present in adipose tissue, heart, and muscle tissue. It is synthesized by extrahepatic tissues, particularly adipocytes, and the gene encoding the protein is situated on chromosome 8p22.
Application
Lipoprotein Lipase from bovine milk has been used:
- as a supplement to test its effect on DiI (1,1′-dioctadecyl-3,3,3′-tetramethyl-indocarbocyanine perchlorate)- very-low-density lipoprotein (VLDL) uptake in breast cancer MDA-MB-231 cells.
- to treat human brain microvascular endothelial cells (HBMECs) for the lipolysis of triglyceride-rich lipoproteins (TGRL).
- to test its effect on gene expression in normal human astrocytes.
- in primary hepatocyte isolation and lipoprotein binding to identify Sulf2 inhibition in T2DM mice for improving diabetic dyslipidemia.
- in transforming growth factor-beta (TGF-β1) immunoassay to test if the TGF-β signaling system regulates the up-regulation and activation of activating transcription factor 3 (ATF3) in human aortic endothelial cells (HAEC) induced by lipolysis products.
- in human TGRL isolation.
- in in vitro lipolysis assay with HSPG-bound LPL, to investigate the effect of human apoE2 (Lys146→Gln) on lipoprotein metabolism.
- in hydrolysis of triglycerides.
- in developing in vitro model of gastrointestinal digestion to investigate the effects of chlorophyll on lipid digestion.
Biochem/physiol Actions
Lipoprotein Lipase (LPL) from bovine milk contributes to maximal lipolytic activity. It associates with casein micelle. LPL regulates triglyceride utilization and displays positional specificity. Lipases, in general, catalyzes the lipolysis of triglycerides especially at the fatty acid in sn-1 and sn-3 positions of the triglyceride.LPL is known to significantly impact the advancement of atherosclerosis. Studies have indicated that advanced atherosclerosis patients display increased LPL mass and activity in their post-heparin plasma.
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.
Physical form
Suspension in 3.8 M ammonium sulfate, 0.02 M Tris HCl, pH 8.0
Preparation Note
Affinity purified
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Biochemistry, Lipoprotein Lipase
Pirahanchi Y, et al.
StatPearls [Internet] (2023)
Y Ikeda et al.
Nihon rinsho. Japanese journal of clinical medicine, 52(12), 3146-3152 (1994-12-01)
We describe molecular and physiological properties of human lipoprotein lipase (LPL) based on recent advanced knowledges. Human LPL is a lipolytic glycoprotein enzyme synthesized by extrahepatic tissues, mainly adipocytes, and its gene is located on chromosome 8p22 with 10 exons
Leslie E Lupien et al.
Journal of lipid research, 61(2), 205-218 (2019-12-07)
We previously described the expression of CD36 and LPL by breast cancer (BC) cells and tissues and the growth-promoting effect of VLDL observed only in the presence of LPL. We now report a model in which LPL is bound to
Richard E Morton et al.
Journal of lipid research, 63(2), 100166-100166 (2022-01-13)
Apolipoprotein F (ApoF) modulates lipoprotein metabolism by selectively inhibiting cholesteryl ester transfer protein activity on LDL. This ApoF activity requires that it is bound to LDL. How hyperlipidemia alters total plasma ApoF and its binding to LDL are poorly understood.
F de Beer et al.
Arteriosclerosis, thrombosis, and vascular biology, 20(7), 1800-1806 (2000-07-15)
The apolipoprotein E2 (Lys146-->Gln) variant is associated with a dominant form of familial dysbetalipoproteinemia. Heterozygous carriers of this variant have elevated levels of plasma triglycerides, cholesterol, and apolipoprotein E (apoE). It was hypothesized that the high amounts of triglycerides in
Articles
Lipid Induced Insulin Resistance
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Protocols
Lipoprotein lipase (LPL) hydrolyzes triglycerides associated with VLDL.
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