L2254
Lipoprotein Lipase from bovine milk
ammonium sulfate suspension, ≥2,000 units/mg protein (BCA)
Sinônimo(s):
LPL, Phospholipase A1, Diacylglycerol acylhydrolase, Diacylglycerol lipase
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R$ 2.888,00
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R$ 11.046,00
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1000 UNITS
R$ 2.888,00
5000 UNITS
R$ 11.046,00
About This Item
Produtos recomendados
fonte biológica
bovine milk
Nível de qualidade
Formulário
ammonium sulfate suspension
atividade específica
≥2,000 units/mg protein (BCA)
temperatura de armazenamento
2-8°C
Descrição geral
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]
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]
Aplicação
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]
Ações bioquímicas/fisiológicas
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]
Definição da unidade
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.
forma física
Suspension in 3.8 M ammonium sulfate, 0.02 M Tris HCl, pH 8.0
Nota de preparo
Affinity purified
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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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.
Biochemistry, Lipoprotein Lipase
Pirahanchi Y, et al.
StatPearls [Internet] (2023)
H Carlijne Hassing et al.
Hepatology (Baltimore, Md.), 55(6), 1746-1753 (2012-01-12)
Type 2 diabetes mellitus (T2DM) impairs hepatic clearance of atherogenic postprandial triglyceride-rich lipoproteins (TRLs). We recently reported that livers from T2DM db/db mice markedly overexpress the heparan sulfate glucosamine-6-O-endosulfatase-2 (SULF2), an enzyme that removes 6-O sulfate groups from heparan sulfate
Artigos
Lipid Induced Insulin Resistance
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Protocolos
Lipoprotein lipase (LPL) hydrolyzes triglycerides associated with VLDL.
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