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LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Additionally we are shipping Lipoprotein Lipase Antibodies (142) and Lipoprotein Lipase Proteins (19) and many more products for this protein.
Showing 10 out of 49 products:
Human Lipoprotein Lipase ELISA Kit for Sandwich ELISA - ABIN366804
Levine, Hull, Buchwald, Villablanca: The spontaneous firing patterns of forebrain neurons. II. Effects of unilateral caudate nuclear ablation. in Brain research 1974
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Guinea Pig Lipoprotein Lipase ELISA Kit - ABIN2345123
Chan, Wong, Pang, Barrett, Watts et al.: Inter-relationships between proprotein convertase subtilisin/kexin type 9, apolipoprotein C-III and plasma apolipoprotein B-48 transport in obese subjects: a stable isotope study in the postprandial ... in Clinical science (London, England : 1979) 2014
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Mouse (Murine) Lipoprotein Lipase ELISA Kit for Sandwich ELISA - ABIN367674
Feng, Hai-ning, Xiao-man, Zun-chen, Sheng-rong, Das: Effect of yellow capsicum extract on proliferation and differentiation of 3T3-L1 preadipocytes. in Nutrition (Burbank, Los Angeles County, Calif.) 2014
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Data show that polymorphisms of rs662799 and rs2266788 in APOA5 (show APOA5 ELISA Kits) gene, rs320 in LPL (show LCP1 ELISA Kits) gene and rs708272 in CETP (show CETP ELISA Kits) gene had significant association with the effect of the lipid-lowering therapy via atorvastatin on ischemic stroke patients.
NOTCH1 (show NOTCH1 ELISA Kits) mutations are tightly associated with LPL (show LCP1 ELISA Kits) gene expression. LPL (show LCP1 ELISA Kits) expression is independently associated with poor outcome in CLL and can be measured as a categorical variable.
Polymorphisms in the LPL (show LCP1 ELISA Kits) gene are associated with increased risk of acute non-biliary pancreatitis.
No significant increase of LPL (show LCP1 ELISA Kits) activity was found at CM and VLDL overload after different kinds of food intake
LPL (show LCP1 ELISA Kits) and PLTP (show PLTP ELISA Kits) appear to be novel glioma-associated proteins and play a role in the progression of human glioma
The acidic domain of GPIHBP1 (show GPIHBP1 ELISA Kits) stabilizes LPL (show LCP1 ELISA Kits) catalytic activity by mitigating the global unfolding of LPL's catalytic domain.
Chronic lymphocytic leukemia patients with high UGT2B17 (show UGT2B17 ELISA Kits) and LPL (show LCP1 ELISA Kits) expression have significantly reduced survival.
Regulation of LPL (show LCP1 ELISA Kits) by the miR (show MLXIP ELISA Kits)-29, miR (show MLXIP ELISA Kits)-1277 and miR (show MLXIP ELISA Kits)-410 that is lost in presence of Hap4, a specific LPL (show LCP1 ELISA Kits) 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 (show UTS2R ELISA Kits) SNPs.
eleterious mutations associated with LPL (show LCP1 ELISA Kits) deficiency
In the present study, the D9N, N291S, and T495G polymorphisms of the LPL (show LCP1 ELISA Kits) gene were not risk factors for the development of CVD.
miR (show MYLIP ELISA Kits)-29b targets LPL and TDG (show TDG ELISA Kits) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
apoC-I (show APOC1 ELISA Kits) and apoC-III (show APOC3 ELISA Kits) 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 ELISA Kits).
ANGPTL4 (show ANGPTL4 ELISA Kits) 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 ELISA Kits).
regions that are responsive to activation by apoC-II (show APOC2 ELISA Kits)
domain (192-238) is absolutely necessary for apolipoprotein AV (show APOA5 ELISA Kits) in lipid binding and lipoprotein lipase activation
feeding induces lipasin, activating the lipasin-Angptl3 (show ANGPTL3 ELISA Kits) pathway, which inhibits LPL in cardiac and skeletal muscles to direct circulating TAG to WAT for storage
MiR (show MLXIP ELISA Kits)-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 ELISA Kits) 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 ELISA Kits) resistance, which is associated with tissue lipid deposition in various insulin (show INS ELISA Kits) target tissues
Results indicated that aggregation of alpha-syn and reduction of UCHL1 (show UCHL1 ELISA Kits) 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 ELISA Kits) on PPARgamma (show PPARG ELISA Kits).
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 ELISA Kits)-deficient (AKO) mice are resistant to diet-induced obesity. Sel1L (show SEL1L ELISA Kits) 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