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The protein encoded by LRAT is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester, an essential reaction for the retinoid cycle in visual system and vitamin A status in liver. Additionally we are shipping LRAT Antibodies (68) and LRAT Kits (5) and many more products for this protein.
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instability of LRAT(E14L) did not abrogate the production of the visual chromophore in a cell-based assay. Instead, expression of LRAT(E14L) led to a rapid increase in cellular levels of retinoic acid upon retinoid supplementation.
LRAT hypermethylation was associated with decreased mRNA levels in colorectal cancer clinical specimens.
lecithin retinol acyltransferase affects all-trans retinoic acid levels and has a role in retinoid sensitivity in malignant melanoma cells.
These findings reveal structural adaptation that facilitates selective catalysis and mechanism responsible for diverse substrate specificity within the LRAT-like enzyme family
high LRAT expression in melanoma might be important in removing retinol as substrate for RA production, thereby inducing signalling pathways leading to dedifferentiation, proliferation and anti-apoptosis
Functional hepatic stellate cells coexpressing both LRAT and CRBP-1 (show RBP1 Proteins), that continue to maintain the ability to store vitamin A, contribute in part to the development of portal and parenchymal fibrogenesis in patients with viral hepatitis.
Lecithin-retinol acyltransferase is a thermostable and highly active enzyme with a likely mode of interfacial activation.
A genetic defect was identified in LRAT as a novel cause of retinitis punctata albescens.
Data show that acyl-modified forms of HRAS (show HRAS Proteins)-like tumor suppressors HRASLS2 (show HRASLS2 Proteins) and HRASLS3 (show PLA2G16 Proteins) mimicking lipolytic activity of lecithin retinol acyltransferase LRAT.
LRAT mutations cause a severe, early childhood onset, progressive retinal dystrophy (show MERTK Proteins).
These experiments are consistent with an expanded role for LRAT function as a protein palmitoyl transferase.
LRAT is not required for isomerase activity beyond synthesis of retinyl-ester substrate, and the association of Rpe65 (show RPE65 Proteins) with membranes is neither dependent upon LRAT nor the result of S-palmitoylation
examined LRAT regulatory region is sufficient to achieve strong and selective expression in the eye and testes but not in liver and other organs
LRAT overexpression diminishes intracellular levels of biologically active retinoids and reduces retinoid antitumor efficacy in the murine melanoma
Mislocalized M-opsin was degraded whereas mislocalized S-opsin (show OPN1SW Proteins) accumulated in Lrat(-/-) cones before the onset of massive ventral/central cone degeneration.
Studies provide mechanistic insights into how vitamin A is distributed to peripheral tissues in a regulated manner and identify LRAT as a critical component of this process.
Lrat KO mice exhibited increased levels of retinoic acid-responsive genes, including p21.
Analyses revealed that LRAT undergoes spontaneous, covalent modification upon incubation with a variety of phosphatidylcholine (show SGMS2 Proteins) substrates. The addition of an acyl chain occurs at the Cys (show DNAJC5 Proteins)(161) residue, indicating formation of a thioester intermediate.
FATP1 inhibits 11-cis (show CISH Proteins) retinol formation via interaction with the visual cycle retinoid isomerase RPE65 (show RPE65 Proteins) and lecithin:retinol acyltransferase
Data show that overexpression of human LRAT specifically in mice oral basal epithelial cells makes these cells more sensitive to carcinogen induced tumorigenesis.
Lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters in the eye and in the liver
LRAT has a role in retinoid absorption and storage
The protein encoded by this gene is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester, an essential reaction for the retinoid cycle in visual system and vitamin A status in liver. Mutations in this gene have been associated with early-onset severe retinal dystrophy.
lecithin retinol acyltransferase
, phosphatidylcholine--retinol O-acyltransferase
, lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase)