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LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Additionally we are shipping Lipoprotein Lipase Kits (61) and Lipoprotein Lipase Proteins (19) and many more products for this protein.
Showing 10 out of 140 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
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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
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Cow (Bovine) Polyclonal Lipoprotein Lipase Primary Antibody for WB - ABIN3043618
Yu, Dai, Chen, Zang, Deng, Liu, Ying: Hypolipidemic and antioxidant activities of polysaccharides from Rosae Laevigatae Fructus in rats. in Carbohydrate polymers 2013
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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
novel mutations cause type 1 hyperlipoproteinemia by inducing a loss or reduction in LPL (show LCP1 Antibodies) secretion accompanied by a loss of LPL (show LCP1 Antibodies) enzymatic activity
LPL (show LCP1 Antibodies) HindIII polymorphism was significantly associated with the risk of coronary artery disease (CAD (show CAD Antibodies)); for Ser447X polymorphism, it was found that only XX genotype was significantly associated with CAD (show CAD Antibodies) risk; PvuII polymorphism had no significant association with CAD (show CAD Antibodies) risk; LPL (show LCP1 Antibodies) HindIII polymorphism might serve as a potential biomarker for CAD (show CAD Antibodies) risk
Rare variants in LPL (show LCP1 Antibodies) and a common variant in APOA5 (show APOA5 Antibodies) were more commonly found in Thai subjects with severe hypertriglyceridemia
apoC-I (show APOC1 Antibodies) inhibited in situ LPL (show LCP1 Antibodies) activity in adipocytes in both a concentration- and time-dependent manner. There was no change in postprandial WAT apoC-I (show APOC1 Antibodies) secretion. WAT apoC-I (show APOC1 Antibodies) secretion may inhibit WAT LPL (show LCP1 Antibodies) activity and promote delayed chylomicron clearance in overweight and obese subjects
isothermal titration calorimetry (ITC) can be used for quantitative measurements of LPL (show LCP1 Antibodies) activity and interactions under in vivo-like conditions, for comparisons of the properties of plasma samples from patients and control subjects as substrates for LPL (show LCP1 Antibodies), as well as for testing of drug candidates developed with the aim to affect the LPL (show LCP1 Antibodies) system.
mAbs RE3 and RG3 bound with reduced affinity to a mutant GPIHBP1 (show GPIHBP1 Antibodies) containing an Ly6 domain mutation (W109S) that abolishes LPL (show LCP1 Antibodies) binding. Immunohistochemistry studies with the GPIHBP1 (show GPIHBP1 Antibodies) mAbs revealed that human GPIHBP1 (show GPIHBP1 Antibodies) is expressed only in capillary endothelial cells. Finally, we created an ELISA that detects GPIHBP1 (show GPIHBP1 Antibodies) in human plasma.
Iotansulin decreased LPL (show LCP1 Antibodies) mRNA levels in HepG2 cells and this was associated with phosphorylation of AKT (show AKT1 Antibodies) and nuclear export of FOXA2 (show FOXA2 Antibodies).
The binding of both antibody 88B8 and GPIHBP1 (show GPIHBP1 Antibodies) to LPL (show LCP1 Antibodies) depends on large segments of LPL's carboxyl-terminal domain.
Loss of Lipoprotein Lipase is associated with Pancreatitis.
In this study, most of the LPL (show LCP1 Antibodies) gene variants were not significantly different in adolescents with normal and elevated triglceryide levels
isothermal titration calorimetry (ITC) can be used for quantitative measurements of LPL activity and interactions under in vivo-like conditions, for comparisons of the properties of plasma samples from patients and control subjects as substrates for LPL, as well as for testing of drug candidates developed with the aim to affect the LPL system.
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
Using in vitro ketosis model by glucose starvation, studied inhibition of ketosis by momilactone B. Found momilactone B could regulate the angiopoietin-like-3 (ANGPTL3 (show ANGPTL3 Antibodies))-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 (show HMGCS2 Antibodies) through the increased expression of STAT5b (show STAT5B Antibodies).
physiological changes in adipose tissue ANGPTL4 (show ANGPTL4 Antibodies) expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4 (show ANGPTL4 Antibodies)(-/-) mice. We conclude that ANGPTL4 (show ANGPTL4 Antibodies) promotes loss of intracellular LPL by stimulating LPL degradation after LPL processing in the endoplasmic reticulum (ER).
LPL moved quickly from heparan sulfate proteoglycans (HSPGs) on adipocytes to GPIHBP1 (show GPIHBP1 Antibodies)-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG (show SDC2 Antibodies)-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 (show GPIHBP1 Antibodies) on endothelial cells
our study reveals that hepatic LPL is involved in the regulation of plasma LPL activity and lipid homeostasis.
The induction of LPL activity by fasting in core transgenic mice activated PPARalpha (show PPARA Antibodies) downstream target genes that are involved in fatty acid beta-oxidation.
This study shows that TNF-alpha (show TNF Antibodies), by a Foxo1 (show FOXO1 Antibodies) dependent pathway, increases the transcription of ANGPTL4 (show ANGPTL4 Antibodies) which is secreted by the cells and causes inactivation of LPL.
Our findings suggest that neuronal LPL is involved in the regulation of body weight and composition in response to either the change in quantity (HF feeding) or quality (n-3 PUFA-enriched) of dietary fat
An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1 (show GPIHBP1 Antibodies).
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.
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