Lecithin Retinol Acyltransferase (Phosphatidylcholine--Retinol O-Acyltransferase) Proteine (LRAT)

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. Zusätzlich bieten wir Ihnen LRAT Antikörper (81) und LRAT Kits (8) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
LRAT 9227 O95237
LRAT 79235 Q9JI60
LRAT 64047 Q9JI61
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Top LRAT Proteine auf antikoerper-online.de

Showing 7 out of 8 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 30 bis 35 Tage
$5,370.21
Details
Insektenzellen Human rho-1D4 tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 0.5 mg Anmelden zum Anzeigen 50 bis 55 Tage
$7,493.38
Details
Insektenzellen Maus rho-1D4 tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 0.25 mg Anmelden zum Anzeigen 50 bis 55 Tage
$5,262.31
Details
Escherichia coli (E. coli) Maus His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 30 bis 35 Tage
$5,370.21
Details
Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 11 bis 12 Tage
$414.29
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Hefe Rind (Kuh) His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$2,467.67
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Hefe Ratte His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$2,467.67
Details

LRAT Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , ,
, ,
Mouse (Murine) ,
,
Rat (Rattus)

Weitere Proteine zu Lecithin Retinol Acyltransferase (Phosphatidylcholine--Retinol O-Acyltransferase) (LRAT) Interaktionspartnern

Human Lecithin Retinol Acyltransferase (Phosphatidylcholine--Retinol O-Acyltransferase) (LRAT) Interaktionspartner

  1. The c.541-15T>G mutation in LRAT results in aberrant splicing and is therefore predicted to be causal for the early onset retinitis pigmentosa in this family.

  2. The genetic analysis performed on our proband showed a novel homozygous mutation on codon 119 of lecithin-cholesterol acyltransferase gene that causes the substitution of glycine by aspartate

  3. 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.

  4. LRAT hypermethylation was associated with decreased mRNA levels in colorectal cancer clinical specimens.

  5. lecithin retinol acyltransferase affects all-trans retinoic acid levels and has a role in retinoid sensitivity in malignant melanoma cells.

  6. These findings reveal structural adaptation that facilitates selective catalysis and mechanism responsible for diverse substrate specificity within the LRAT-like enzyme family

  7. 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

  8. Functional hepatic stellate cells coexpressing both LRAT and CRBP-1, 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.

  9. Lecithin-retinol acyltransferase is a thermostable and highly active enzyme with a likely mode of interfacial activation.

  10. A genetic defect was identified in LRAT as a novel cause of retinitis punctata albescens.

  11. Data show that acyl-modified forms of HRAS-like tumor suppressors HRASLS2 and HRASLS3 mimicking lipolytic activity of lecithin retinol acyltransferase LRAT.

  12. LRAT mutations cause a severe, early childhood onset, progressive retinal dystrophy.

  13. This study showed that malignant melanoma cells are able to esterify all-trans retinol and subsequently isomerize all-trans retinyl esters (RE) into 11-cis retinol, whereas their benign counterparts-melanocytes are not able to catalyze these reactions.

  14. Data show that overexpression of human LRAT specifically in mice oral basal epithelial cells makes these cells more sensitive to carcinogen induced tumorigenesis.

  15. LRAT expression is higher in renal tumors with an indolent biological behavior

  16. Conserved residues Cys-161 and His-60 form the essential catalytic dyad of LRAT that represents a novel thiol protease motif, which functions in an acyltransferase reaction.

  17. LRAT has a role in preventing progression of invasive bladder cancer

  18. Results provide evidence that multiple LRAT mRNA transcripts, which are 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.

  19. LRAT has a role in retinoid absorption and storage

  20. These experiments are consistent with an expanded role for LRAT function as a protein palmitoyl transferase.

Cow (Bovine) Lecithin Retinol Acyltransferase (Phosphatidylcholine--Retinol O-Acyltransferase) (LRAT) Interaktionspartner

  1. These experiments are consistent with an expanded role for LRAT function as a protein palmitoyl transferase.

  2. LRAT is not required for isomerase activity beyond synthesis of retinyl-ester substrate, and the association of Rpe65 with membranes is neither dependent upon LRAT nor the result of S-palmitoylation

Mouse (Murine) Lecithin Retinol Acyltransferase (Phosphatidylcholine--Retinol O-Acyltransferase) (LRAT) Interaktionspartner

  1. examined LRAT regulatory region is sufficient to achieve strong and selective expression in the eye and testes but not in liver and other organs

  2. LRAT overexpression diminishes intracellular levels of biologically active retinoids and reduces retinoid antitumor efficacy in the murine melanoma

  3. Mislocalized M-opsin was degraded whereas mislocalized S-opsin accumulated in Lrat(-/-) cones before the onset of massive ventral/central cone degeneration.

  4. 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.

  5. Lrat KO mice exhibited increased levels of retinoic acid-responsive genes, including p21.

  6. Analyses revealed that LRAT undergoes spontaneous, covalent modification upon incubation with a variety of phosphatidylcholine substrates. The addition of an acyl chain occurs at the Cys(161) residue, indicating formation of a thioester intermediate.

  7. FATP1 inhibits 11-cis retinol formation via interaction with the visual cycle retinoid isomerase RPE65 and lecithin:retinol acyltransferase

  8. Data show that overexpression of human LRAT specifically in mice oral basal epithelial cells makes these cells more sensitive to carcinogen induced tumorigenesis.

  9. Lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters in the eye and in the liver

  10. LRAT has a role in retinoid absorption and storage

  11. LRAT-/- mice are much more susceptible to vitamin A deficiency and should be an excellent animal model of vitamin A deficiency

  12. analysis of the topology and subcellular localization of LRAT, a critical enzyme in vitamin A metabolism

  13. LRAT is not required for isomerase activity beyond synthesis of retinyl-ester substrate, and the association of Rpe65 with membranes is neither dependent upon LRAT nor the result of S-palmitoylation

  14. Three Lrat mouse lines with genetic modifications were generated. This feature allows the disruption of this gene in any tissue of choice, by intercrossing with mice in which Cre-recombinase expression is driven by an appropriate tissue-specific promoter.

  15. LRAT acts together with Cyp26A1, one of the enzymes that catalyze the degradation of retinoic acid, and possibly with STRA6, the recently identified cell surface receptor for retinol-RBP

  16. These data show that the Lrat-/- and Rpe65-/- mice are comparable models for studies of Leber congenital amaurosis and that the destructive cone opsin mistrafficking is caused by the lack of 11-cis retinal.

  17. proximal region together with basal transcription factors may be sufficient to drive Lrat expression.

LRAT Protein Überblick

Protein Überblick

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.

Genbezeichner und Symbole assoziert mit LRAT

  • lecithin retinol acyltransferase (LRAT)
  • lecithin-retinol acyltransferase (phosphatidylcholine-retinol-O-acyltransferase) (Lrat)
  • lecithin retinol acyltransferase (Lrat)
  • 1300010A18Rik Protein
  • AI449251 Protein
  • LCA14 Protein

Bezeichner auf Proteinebene für LRAT

lecithin retinol acyltransferase , phosphatidylcholine--retinol O-acyltransferase , phosphatidylcholine-retinol-O-acyltransferase , lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase)

GENE ID SPEZIES
9227 Homo sapiens
281285 Bos taurus
79235 Mus musculus
64047 Rattus norvegicus
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