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Dietary fats are packaged by intestine into triglyceride-rich lipoproteins called chylomicrons. Additionally we are shipping GPIHBP1 Antibodies (57) and GPIHBP1 Kits (8) and many more products for this protein.
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The acidic domain of GPIHBP1 stabilizes LPL (show LCP1 Proteins) catalytic activity by mitigating the global unfolding of LPL's catalytic domain.
2 novel GPIHBP1 missense mutations in 2 unrelated patients as the cause of their severe hypertriglyceridemia
GPIHBP1 mutations should be considered in neonates with chylomicronemia negative for mutations in LPL (show LCP1 Proteins) gene
the two domains of GPIHBP1 interact independently with LPL (show LCP1 Proteins) and the functionality of LPL (show LCP1 Proteins) depends on its localization on GPIHBP1
No GPIHBP1 mutations were identified in a cohort of patients with diabetic lipemia.
GPIHBP1 missense mutations leading to protein multimerization prevent lipoprotein lipase (show LPL Proteins) binding.
Homozygosity for a deletion of exons 3 and 4 of GPIHBP1 results in Type 1 hyperlipoproteinemia.
an extra cysteine in the GPIHBP1 Ly6 motif results in multimerization of GPIHBP1, defective LPL (show LCP1 Proteins) binding, and severe hypertriglyceridemia.
Wild-type lipoprotein lipase (LPL (show LPL Proteins)) and a mutated (S447X-LPL (show LCP1 Proteins)) protein bind to the endothelial cell LPL (show LCP1 Proteins) transporter GPIHBP1 with equal efficiency.
A polymorphism in the GPIHBP1 gene promoter was associated with an increased risk of hypertriglyceridemia and had an additive effect on the risk conferred by LPL (show LCP1 Proteins) defective alleles.
Laminin regulates PDGFRbeta cell differentiation, fate determination, cell stemness and muscle development via gpihbp1.
the two domains of GPIHBP1 interact independently with LPL (show LPL Proteins) and the functionality of LPL (show LPL Proteins) depends on its localization on GPIHBP1
TRL margination depends on LPL (show LPL Proteins) bound to GPIHBP1.
In adipose tissue, Gpihbp1 levels increases rapidly during fasting, when lipoprotein lipase (show LPL Proteins) activity decreases.
Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL (show LPL Proteins) or GPIHBP1 in mouse pancreas.
The GPIHBP1 and LPL (show LPL Proteins) move bidirectionally across endothelial cells in vesicles and that transport is efficient even when caveolin-1 (show CAV1 Proteins) is absent.
analysis of glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) expression in mouse tissues revealed by positron emission tomography scanning
Intravenously injected apoA-V (show APOA5 Proteins) rHDL significantly lowers plasma TG in an apoA-V (show APOA5 Proteins) deficient mouse model and requires gpihbp1.
GPIHBP1 is located at the basolateral surface of capillary endothelial cells and actively transports LPL (show LPL Proteins) across endothelial cells.
Like ANGPTL4 (show ANGPTL4 Proteins), ANGPTL3 (show ANGPTL3 Proteins) inhibited nonstabilized LPL (show LPL Proteins) but not GPIHBP1-stabilized LPL (show LPL Proteins)
Dietary fats are packaged by intestine into triglyceride-rich lipoproteins called chylomicrons. The triglycerides in chylomicrons are hydrolyzed by lipoprotein lipase (LPL: MIM 609708) along the luminal surface of capillaries, mainly in heart, skeletal muscle, and adipose tissue. GPIHBP1 is a capillary endothelial cell protein that provides a platform for LPL-mediated processing of chylomicrons (Beigneux et al., 2007
glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
, GPI-anchored HDL-binding protein 1
, glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
, GPI anchored high density lipoprotein binding protein 1
, high density lipoprotein-binding protein 1