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LCAT encodes the extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. Additionally we are shipping LCAT Antibodies (117) and LCAT Kits (47) and many more products for this protein.
Showing 10 out of 34 products:
data suggests a model wherein the active site of LCAT is shielded from soluble substrates by a dynamic lid until it interacts with HDL (show HSD11B1 Proteins) to allow transesterification to proceed
Increased LCAT activity may be associated with increased formation of triglyceride rich lipoproteins, leading to a reduction in LDL particle size and atherosclerosis.
Mapping the naturally occurring mutations onto the structure provides insight into how they may affect LCAT enzymatic activity.
Report slightly reduction in LCAT that would probably reflect a delay in reverse cholesterol transport occurring in MetS.
rs5923 polymorphism is not associated with low high-density lipoprotein cholesterol(HDL (show HSD11B1 Proteins)-C)levels in Iranian population
increased cholesterol esterification by LCAT is atheroprotective
The data indicate that this novel apoA-I (show APOA1 Proteins) missense is associated with markedly decreased levels of HDL (show HSD11B1 Proteins) cholesterol and very large alpha-1 HDL (show HSD11B1 Proteins), as well as decreased serum cellular cholesterol efflux and LCAT activity
A robust all-atom model for LCAT generated by homology modeling
This study investigated how the natural LCAT[T147I] and LCAT[P274S] mutations affect the pathway of biogenesis of high-density lipoproteins.
A synonymous H287H mutation in the coding region of exon 6 of the lecithin cholesterol acyltransferase gene was observed in an individual with HDLC levels of 75 mg/dl.
Taken together, these results suggest that apoE (show APOE Proteins)-containing discoidal HDLs (show CSF1R Proteins) do not require LCAT-dependent maturation to mediate efficient Abeta (show APP Proteins) clearance
Gene transfer of WT LCAT in LCAT(-/-) mice increased 11.8-fold the plasma cholesterol, whereas the LCAT[T147I] and LCAT[P274S] mutants caused a 5.2- and 2.9-fold increase, respectively.
DYRK1A (show DYRK1A Proteins) overexpression decreases plasma lecithin:cholesterol acyltransferase activity and apolipoprotein A-I (show APOA1 Proteins) levels.
adrenal glucocorticoid function in LCAT knockout (KO) mice
a novel function of apoA-IV (show APOA4 Proteins) in the biogenesis of discrete HDL (show HSD11B1 Proteins)-A-IV particles with the participation of ABCA1 (show ABCA1 Proteins) and LCAT
Studies suggest that absence of lecithin cholesterol acyltransferase (LCAT) may protect against insulin (show INS Proteins) resistance, diabetes and obesity.
Data show that LCAT activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2 (show SPTLC2 Proteins))+/- and sphingomyelin synthase 2 (Sms2 (show SGMS2 Proteins))-/- mice, but markedly lower in ApoE (show APOE Proteins)-/- and Ldlr (show LDLR Proteins)-/- mice.
LCAT deficiency confers gender-specific protection against diet-induced obesity and insulin (show INS Proteins) resistance at least in part through regulation in UPR, white adipose tissue adipogenesis, and brown adipocyte partitioning
Oxidative stress is markedly elevated in lecithin:cholesterol acyltransferase-deficient mice and is paradoxically reversed in the apolipoprotein E (show APOE Proteins) knockout background in association with a reduction in atherosclerosis
LCAT cholesterol esterification is associated with the increase of ApoE (show APOE Proteins)/ApoA-I (show APOA1 Proteins) ratio during atherosclerosis progression in rabbit.
The 1,434 bp mRNA sequence of porcine LCAT including the full coding region and encoding a protein of 472 amino acids, was obtained.
This gene encodes the extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. Mutations in this gene have been found to cause fish-eye disease as well as LCAT deficiency.
, phospholipid-cholesterol acyltransferase
, lecithin-cholesterol acyltransferase Lcat
, lecithin-cholesterol acyltransferase
, lecithin cholesterol acyltransferase
, Lecithin-cholesterol acyltransferase