LRAT Antibody, HRP conjugated
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Product Specs
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Typically, we can ship your order within 1-3 business days after receiving it. Delivery times may vary depending on the purchase method and location. For specific delivery timelines, please consult your local distributors.
Synonyms
LRAT; Lecithin retinol acyltransferase; Phosphatidylcholine--retinol O-acyltransferase
Target Names
LRAT
Uniprot No.
Target Background
Function
Lecithin-retinol acyltransferase (LRAT) catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, resulting in the production of all-trans retinyl esters. These esters serve as storage forms of vitamin A. LRAT plays a crucial role in vision. It provides the necessary all-trans retinyl ester substrates for the isomerohydrolase, which subsequently processes them into 11-cis-retinol within the retinal pigment epithelium. This 11-cis-retinol is then oxidized and converted into 11-cis-retinaldehyde by a membrane-associated alcohol dehydrogenase. 11-cis-retinaldehyde acts as the chromophore for rhodopsin and the cone photopigments, crucial for vision. LRAT is essential for the survival of cone photoreceptors and the maintenance of proper rod photoreceptor cell morphology.
Gene References Into Functions
- Genetic analysis of a proband revealed a novel homozygous mutation on codon 119 of the lecithin-cholesterol acyltransferase gene, leading to the substitution of glycine with aspartate. PMID: 28942093
- The instability of LRAT(E14L) did not hinder the production of the visual chromophore in a cell-based assay. Instead, expression of LRAT(E14L) resulted in a rapid increase in cellular levels of retinoic acid upon retinoid supplementation. PMID: 28758396
- LRAT hypermethylation was associated with decreased mRNA levels in colorectal cancer clinical specimens. PMID: 25260806
- Lecithin retinol acyltransferase influences all-trans retinoic acid levels and plays a role in retinoid sensitivity in malignant melanoma cells. PMID: 25236354
- Research has uncovered structural adaptations that facilitate selective catalysis and the mechanism responsible for diverse substrate specificity within the LRAT-like enzyme family. PMID: 25383759
- High LRAT expression in melanoma may be important in removing retinol as a substrate for RA production, potentially inducing signaling pathways that lead to dedifferentiation, proliferation, and anti-apoptosis. PMID: 24433184
- Functional hepatic stellate cells co-expressing both LRAT and CRBP-1, which maintain the ability to store vitamin A, contribute to the development of portal and parenchymal fibrogenesis in individuals with viral hepatitis. PMID: 23890161
- Lecithin-retinol acyltransferase is a thermostable and highly active enzyme, likely exhibiting interfacial activation. PMID: 24613493
- A genetic defect in LRAT has been identified as a novel cause of retinitis punctata albescens. PMID: 22559933
- Data suggests that acyl-modified forms of HRAS-like tumor suppressors HRASLS2 and HRASLS3 mimic the lipolytic activity of lecithin retinol acyltransferase (LRAT). PMID: 22605381
- LRAT mutations cause a severe, early childhood onset, progressive retinal dystrophy. PMID: 22570351
- Research has shown that malignant melanoma cells can esterify all-trans retinol and subsequently isomerize all-trans retinyl esters (RE) into 11-cis retinol, while their benign counterparts, melanocytes, are unable to catalyze these reactions. PMID: 21465477
- Overexpression of human LRAT specifically in mice oral basal epithelial cells has been found to increase these cells' sensitivity to carcinogen-induced tumorigenesis. PMID: 19471114
- LRAT expression is higher in renal tumors with an indolent biological behavior. PMID: 14581364
- Conserved residues Cys-161 and His-60 form the essential catalytic dyad of LRAT, representing a novel thiol protease motif that functions in an acyltransferase reaction. PMID: 14596594
- LRAT plays a role in preventing the progression of invasive bladder cancer. PMID: 15161698
- Evidence suggests that multiple LRAT mRNA transcripts, expressed in a tissue-specific manner, may result from differential splicing of the 5'UTR region and the use of multiple polyadenylation signals in the 3'UTR. PMID: 15474300
- LRAT is involved in retinoid absorption and storage. PMID: 16115871
- Experimental findings are consistent with an expanded role for LRAT function as a protein palmitoyl transferase. PMID: 16939223
- The phenotype of patients with mutations in LRAT is similar to that of patients with mutations in RPE65, suggesting the need for systematic screening of both genes in cases of typical phenotype. PMID: 17011878
- LRAT mutations are likely a rare cause of Leber congenital amaurosis among patients from North America. PMID: 17438524
- Lecithin: retinol acyltransferase protein is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver. PMID: 18544127
- Transcriptional regulation is aberrant in human prostate cancer and involves GATA transcription factors in normal prostate epithelial cells. PMID: 18652909
- The proximal region, together with basal transcription factors, may be sufficient to drive Lrat expression. PMID: 19665987
Database Links
Involvement In Disease
Leber congenital amaurosis 14 (LCA14)
Protein Families
H-rev107 family
Subcellular Location
Endoplasmic reticulum membrane; Single-pass membrane protein. Rough endoplasmic reticulum. Endosome, multivesicular body. Cytoplasm, perinuclear region.
Tissue Specificity
Hepatic stellate cells and endothelial cells (at protein level). Found at high levels in testis and liver, followed by retinal pigment epithelium, small intestine, prostate, pancreas and colon. Low expression observed in brain. In fetal tissues, expressed
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