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L2254

Sigma-Aldrich

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

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Pricing and availability is not currently available.

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.[1]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.[2] It is synthesized by extrahepatic tissues, particularly adipocytes, and the gene encoding the protein is situated on chromosome 8p22.[3]

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.[4]
  • to treat human brain microvascular endothelial cells (HBMECs) for the lipolysis of triglyceride-rich lipoproteins (TGRL).[5]
  • to test its effect on gene expression in normal human astrocytes.[6]
  • in primary hepatocyte isolation and lipoprotein binding to identify Sulf2 inhibition in T2DM mice for improving diabetic dyslipidemia.[7]
  • 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.[8]
  • in human TGRL isolation.[9]
  • in in vitro lipolysis assay with HSPG-bound LPL, to investigate the effect of human apoE2 (Lys146→Gln) on lipoprotein metabolism.[10]
  • in hydrolysis of triglycerides.[11]
  • in developing in vitro model of gastrointestinal digestion to investigate the effects of chlorophyll on lipid digestion.[12]

Biochem/physiol Actions

Lipoprotein Lipase (LPL) from bovine milk contributes to maximal lipolytic activity.[1] It associates with casein micelle. LPL regulates triglyceride utilization[13] and displays positional specificity.[1] Lipases, in general, catalyzes the lipolysis of triglycerides especially at the fatty acid in sn-1 and sn-3 positions of the triglyceride.[1]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.[2]

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

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    Biochemistry, Lipoprotein Lipase
    Pirahanchi Y, et al.
    StatPearls [Internet] (2023)
    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
    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
    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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