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LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Additionally we are shipping Lipoprotein Lipase Antibodies (138) and Lipoprotein Lipase Kits (46) and many more products for this protein.
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The acidic domain of GPIHBP1 (show GPIHBP1 Proteins) stabilizes LPL (show LCP1 Proteins) catalytic activity by mitigating the global unfolding of LPL's catalytic domain.
Chronic lymphocytic leukemia patients with high UGT2B17 and LPL (show LCP1 Proteins) expression have significantly reduced survival.
Regulation of LPL by the miR-29, miR-1277 and miR-410 that is lost in presence of Hap4, a specific LPL TG-lowering haplotype. Consequently p.Ser474Ter association with TG concentration could be at least partially explained by its strong linkage disequilibrium with these functional 3'UTR SNPs.
eleterious mutations associated with LPL (show LCP1 Proteins) deficiency
In the present study, the D9N, N291S, and T495G polymorphisms of the LPL (show LCP1 Proteins) gene were not risk factors for the development of CVD.
Despite the considerable metabolic changes accompanying pregnancy, the triglyceride-lowering effect associated with the -93GG LPL (show LCP1 Proteins) genotype in African Americans persists during late pregnancy
Polymorphisms rs328 and rs268 of the lipoprotein lipase gene do not affect the occurrence of NAFLD in women with PCOS or without PCOS.
lipoprotein lipase polymorphism was not associated with the incidence of coronary heart disease in Sudan.
Individuals carrying the lipoprotein lipase (LPL) rs12678919 polymorphism (A --> G) had no significant change in the risk of developing AMD (show AMD1 Proteins).
Asn291Ser(rs268), HindIII(rs320) and Ser447Ter(rs328) polymorphisms of lipoprotein lipase were associated with a risk of Alzheimer disease.[meta-analysis]
miR (show MYLIP Proteins)-29b targets LPL and TDG (show TDG Proteins) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
apoC-I (show APOC1 Proteins) and apoC-III (show APOC3 Proteins) inhibit lipolysis by displacing LPL from lipid emulsion particles. We also propose a role for these apolipoproteins in the irreversible inactivation of LPL by factors such as angptl4 (show ANGPTL4 Proteins).
ANGPTL4 (show ANGPTL4 Proteins) is more accurately described as a reversible, noncompetitive inhibitor of LPL.
Our findings confirmed that three novel SNPs we identified in the LPL gene can affect fatty acid composition and carcass traits. Therefore, selection for AA and GA genotypes should be recommended to genetically improve beef quality and flavor.
Single nucleotide polymorphisms of the LPL gene might be useful genetic markers for growth traits in the bovine reproduction and breeding.
Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII (show APOC2 Proteins).
regions that are responsive to activation by apoC-II (show APOC2 Proteins)
domain (192-238) is absolutely necessary for apolipoprotein AV (show APOA5 Proteins) in lipid binding and lipoprotein lipase activation
feeding induces lipasin, activating the lipasin-Angptl3 (show ANGPTL3 Proteins) pathway, which inhibits LPL in cardiac and skeletal muscles to direct circulating TAG to WAT for storage
MiR (show MLXIP Proteins)-590 agomir down-regulates LPL mRNA and protein expression in a mouse model of atherosclerosis.
Deficiency of Lipoprotein Lipase in Neurons Decreases AMPA (show GRIA3 Proteins) Receptor Phosphorylation and Leads to Neurobehavioral Abnormalities in Mice
Systemic LPL deletion results in impaired glucose tolerance, whole-body and tissue-specific insulin (show INS Proteins) resistance, which is associated with tissue lipid deposition in various insulin (show INS Proteins) target tissues
Results indicated that aggregation of alpha-syn and reduction of UCHL1 (show UCHL1 Proteins) expression in LPL-deficient mice may affect synaptic function.
the amount of LPL expressed in muscle and heart governed both the binding of chylomicron particles and the assimilation of chylomicron lipids in the tissue.
Maternal overnutrition induces LPL expression in trophoblasts by reducing the inhibitory effect of SIRT1 (show SIRT1 Proteins) on PPARgamma (show PPARG Proteins).
Lipoprotein lipase is an important modulator of lipid uptake and storage in hypothalamic neurons.
Results suggest that impaired synaptic vesicle recycling results from deficient docosahexaenoic acid and arachidonic acid and contributes to the presynaptic dysfunction and plasticity impairment in LPL-deficient neurons
Adipocyte-specific Sel1L (show SEL1L Proteins)-deficient (AKO) mice are resistant to diet-induced obesity. Sel1L (show SEL1L Proteins) stabilizes and prevents LPL dimers from aggregation in the endoplasmic reticulum.
LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism.
, O 1-4-5
, adipose lipoprotein lipase
, triacylglycerol lipase