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LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Additionally we are shipping Lipoprotein Lipase Kits (66) and Lipoprotein Lipase Proteins (15) 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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Human Polyclonal Lipoprotein Lipase Primary Antibody for WB - ABIN4331137
Zhang, Cui, Wang, Shang, Qi, Xue, Zhao, Deng, Xie: PPARα/γ agonists and antagonists differently affect hepatic lipid metabolism, oxidative stress and inflammatory cytokine production in steatohepatitic rats. in Cytokine 2015
Chicken Monoclonal Lipoprotein Lipase Primary Antibody for IP, ELISA - ABIN2475334
Peterson, Fujimoto, Brunzell: Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies. in Journal of lipid research 1992
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Chicken Monoclonal Lipoprotein Lipase Primary Antibody for Func, IP - ABIN2475336
Chang, Reich, Brunzell, Will: Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2. in Journal of lipid research 1999
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Chicken Monoclonal Lipoprotein Lipase Primary Antibody for IP, ELISA - ABIN2475333
Hussain, Obunike, Shaheen, Hussain, Shelness, Goldberg: High affinity binding between lipoprotein lipase and lipoproteins involves multiple ionic and hydrophobic interactions, does not require enzyme activity, and is modulated by glycosaminoglycans. in The Journal of biological chemistry 2000
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The expression of COBLL1, LPL, and ZAP70 corresponded to patient prognosis and to IGHV mutational status, although not absolutely. When we combined all three markers together and performed the ROC analysis, AUC increased compared to the AUC of individual gene expression.
heterozygous N291S mutation in the lipoprotein lipase gene impairs whole-body insulin (show INS Antibodies) sensitivity and affects a distinct set of plasma metabolites in humans
LPL (show LCP1 Antibodies) is important for the maturation of small discoidal HDL (show HSD11B1 Antibodies) particles into large spherical HDL (show HSD11B1 Antibodies) particles, while HL is important for HDL (show HSD11B1 Antibodies) remodeling of very large HDL (show HSD11B1 Antibodies) particles into intermediate-size HDL (show HSD11B1 Antibodies) particles, as shown in lipoprotein lipase and hepatic lipase (show LIPC Antibodies) deficiency
The authors now show: (1) that ANGPTL4 (show ANGPTL4 Antibodies) inactivates LPL (show LCP1 Antibodies) by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 (show GPIHBP1 Antibodies) renders LPL (show LCP1 Antibodies) largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 (show GPIHBP1 Antibodies) are required for this protective effect.
Carrier status for the two common LPL (show LCP1 Antibodies) variants: 447Ter (low TG/high HDL (show HSD11B1 Antibodies)-C) and 291Ser (high TG/low HDL (show HSD11B1 Antibodies)-C) was determined. Compared with the reference variant, the prevalence of metabolic syndrome was lower in carriers of the 447Ter variant (11.2% vs. 17.9%, P < 0.001) but with no difference in carriers of the 291Ser variant (18.4% vs. 16.5%, P = 0.59).
A rare variant in APOC3 (show APOC3 Antibodies)(rs138326449) has been associated with triglyceride, very low-density lipoprotein, and high-density lipoprotein levels, as well as risk of coronary heart disease. Effects are unlikely to be solely predictable by the action of APOC3 (show APOC3 Antibodies) through LPL (show LCP1 Antibodies).
LPL (show LCP1 Antibodies) gene polymorphisms are not genetic markers for the development of stroke in the Colombian sample used.
Acute hypoxia strongly inhibits lipoprotein lipase activity in differentiated human preadipocytes.
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
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
The data suggests that ANGPTL3 (show ANGPTL3 Antibodies) is part of the machinery causing dyslipidemia majorily via LPL inhibition in mastitis mice.
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
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