Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Zusätzlich bieten wir Ihnen Lipoprotein Lipase Kits (66) und Lipoprotein Lipase Proteine (15) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 140 products:
Cat (Feline) Monoclonal Lipoprotein Lipase Primary Antibody für 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 Pubmed References
Human Monoclonal Lipoprotein Lipase Primary Antibody für 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 Pubmed References
Cow (Bovine) Polyclonal Lipoprotein Lipase Primary Antibody für 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
Show all 2 Pubmed References
Human Polyclonal Lipoprotein Lipase Primary Antibody für 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 für 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
Show all 3 Pubmed References
Chicken Monoclonal Lipoprotein Lipase Primary Antibody für 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
Show all 3 Pubmed References
Chicken Monoclonal Lipoprotein Lipase Primary Antibody für 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
Show all 3 Pubmed References
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 (zeige INS Antikörper) sensitivity and affects a distinct set of plasma metabolites in humans
LPL (zeige LCP1 Antikörper) is important for the maturation of small discoidal HDL (zeige HSD11B1 Antikörper) particles into large spherical HDL (zeige HSD11B1 Antikörper) particles, while HL is important for HDL (zeige HSD11B1 Antikörper) remodeling of very large HDL (zeige HSD11B1 Antikörper) particles into intermediate-size HDL (zeige HSD11B1 Antikörper) particles, as shown in lipoprotein lipase and hepatic lipase (zeige LIPC Antikörper) deficiency
The authors now show: (1) that ANGPTL4 (zeige ANGPTL4 Antikörper) inactivates LPL (zeige LCP1 Antikörper) by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 (zeige GPIHBP1 Antikörper) renders LPL (zeige LCP1 Antikörper) largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 (zeige GPIHBP1 Antikörper) are required for this protective effect.
Carrier status for the two common LPL (zeige LCP1 Antikörper) variants: 447Ter (low TG/high HDL (zeige HSD11B1 Antikörper)-C) and 291Ser (high TG/low HDL (zeige HSD11B1 Antikörper)-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 (zeige APOC3 Antikörper)(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 (zeige APOC3 Antikörper) through LPL (zeige LCP1 Antikörper).
LPL (zeige LCP1 Antikörper) 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 (zeige LCP1 Antikörper) secretion accompanied by a loss of LPL (zeige LCP1 Antikörper) enzymatic activity
LPL (zeige LCP1 Antikörper) HindIII polymorphism was significantly associated with the risk of coronary artery disease (CAD (zeige CAD Antikörper)); for Ser447X polymorphism, it was found that only XX genotype was significantly associated with CAD (zeige CAD Antikörper) risk; PvuII polymorphism had no significant association with CAD (zeige CAD Antikörper) risk; LPL (zeige LCP1 Antikörper) HindIII polymorphism might serve as a potential biomarker for CAD (zeige CAD Antikörper) 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 (zeige MYLIP Antikörper)-29b targets LPL and TDG (zeige TDG Antikörper) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
apoC-I (zeige APOC1 Antikörper) and apoC-III (zeige APOC3 Antikörper) 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 (zeige ANGPTL4 Antikörper).
ANGPTL4 (zeige ANGPTL4 Antikörper) 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 (zeige APOC2 Antikörper).
regions that are responsive to activation by apoC-II (zeige APOC2 Antikörper)
domain (192-238) is absolutely necessary for apolipoprotein AV (zeige APOA5 Antikörper) in lipid binding and lipoprotein lipase activation
The data suggests that ANGPTL3 (zeige ANGPTL3 Antikörper) 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 (zeige ANGPTL3 Antikörper))-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 (zeige HMGCS2 Antikörper) through the increased expression of STAT5b (zeige STAT5B Antikörper).
physiological changes in adipose tissue ANGPTL4 (zeige ANGPTL4 Antikörper) expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4 (zeige ANGPTL4 Antikörper)(-/-) mice. We conclude that ANGPTL4 (zeige ANGPTL4 Antikörper) 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 (zeige GPIHBP1 Antikörper)-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG (zeige SDC2 Antikörper)-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 (zeige GPIHBP1 Antikörper) 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 (zeige PPARA Antikörper) downstream target genes that are involved in fatty acid beta-oxidation.
This study shows that TNF-alpha (zeige TNF Antikörper), by a Foxo1 (zeige FOXO1 Antikörper) dependent pathway, increases the transcription of ANGPTL4 (zeige ANGPTL4 Antikörper) 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 (zeige GPIHBP1 Antikörper).
feeding induces lipasin, activating the lipasin-Angptl3 (zeige ANGPTL3 Antikörper) 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