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LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Additionally we are shipping Lipoprotein Lipase Kits (49) and Lipoprotein Lipase Proteins (19) and many more products for this protein.
Showing 10 out of 143 products:
Cat (Feline) Monoclonal Lipoprotein Lipase Primary Antibody for ELISA, FACS - ABIN1042621
Peterson, Ayyobi, Ma, Henderson, Reina, Deeb, Santamarina-Fojo, Hayden, Brunzell: Structural and functional consequences of missense mutations in exon 5 of the lipoprotein lipase gene. in Journal of lipid research 2002
Show all 4 references for ABIN1042621
Human Monoclonal Lipoprotein Lipase Primary Antibody for ELISA, WB - ABIN969262
Berk, Johnson, Lee, Zhang, Boozer, Pi-Sunyer, Fried, Albu: Higher post-absorptive skeletal muscle LPL activity in African American vs. non-Hispanic White pre-menopausal women. in Obesity (Silver Spring, Md.) 2008
Show all 2 references for ABIN969262
Cow (Bovine) Monoclonal Lipoprotein Lipase Primary Antibody for EIA, Func - ABIN125994
Voyta, Via, Kinnunen, Sparrow, Gotto, Smith: Monoclonal antibodies against bovine milk lipoprotein lipase. Characterization of an antibody specific for the apolipoprotein C-II binding site. in The Journal of biological chemistry 1985
Data show that polymorphisms of rs662799 and rs2266788 in APOA5 (show APOA5 Antibodies) gene, rs320 in LPL (show LCP1 Antibodies) gene and rs708272 in CETP (show CETP Antibodies) gene had significant association with the effect of the lipid-lowering therapy via atorvastatin on ischemic stroke patients.
NOTCH1 (show NOTCH1 Antibodies) mutations are tightly associated with LPL (show LCP1 Antibodies) gene expression. LPL (show LCP1 Antibodies) expression is independently associated with poor outcome in CLL and can be measured as a categorical variable.
Polymorphisms in the LPL (show LCP1 Antibodies) gene are associated with increased risk of acute non-biliary pancreatitis.
No significant increase of LPL (show LCP1 Antibodies) activity was found at CM and VLDL overload after different kinds of food intake
LPL (show LCP1 Antibodies) and PLTP (show PLTP Antibodies) appear to be novel glioma-associated proteins and play a role in the progression of human glioma
The acidic domain of GPIHBP1 (show GPIHBP1 Antibodies) stabilizes LPL (show LCP1 Antibodies) catalytic activity by mitigating the global unfolding of LPL's catalytic domain.
Chronic lymphocytic leukemia patients with high UGT2B17 and LPL (show LCP1 Antibodies) expression have significantly reduced survival.
Regulation of LPL (show LCP1 Antibodies) by the miR (show MLXIP Antibodies)-29, miR (show MLXIP Antibodies)-1277 and miR (show MLXIP Antibodies)-410 that is lost in presence of Hap4, a specific LPL (show LCP1 Antibodies) 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 Antibodies) SNPs.
eleterious mutations associated with LPL (show LCP1 Antibodies) deficiency
In the present study, the D9N, N291S, and T495G polymorphisms of the LPL (show LCP1 Antibodies) gene were not risk factors for the development of CVD.
miR (show MYLIP Antibodies)-29b targets LPL and TDG (show TDG Antibodies) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
apoC-I (show APOC1 Antibodies) and apoC-III (show APOC3 Antibodies) 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 Antibodies).
ANGPTL4 (show ANGPTL4 Antibodies) 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 Antibodies).
regions that are responsive to activation by apoC-II (show APOC2 Antibodies)
domain (192-238) is absolutely necessary for apolipoprotein AV (show APOA5 Antibodies) in lipid binding and lipoprotein lipase activation
feeding induces lipasin, activating the lipasin-Angptl3 (show ANGPTL3 Antibodies) pathway, which inhibits LPL in cardiac and skeletal muscles to direct circulating TAG to WAT for storage
MiR (show MLXIP Antibodies)-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 Antibodies) 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 Antibodies) resistance, which is associated with tissue lipid deposition in various insulin (show INS Antibodies) target tissues
Results indicated that aggregation of alpha-syn and reduction of UCHL1 (show UCHL1 Antibodies) 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 Antibodies) on PPARgamma (show PPARG Antibodies).
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 Antibodies)-deficient (AKO) mice are resistant to diet-induced obesity. Sel1L (show SEL1L Antibodies) 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