LRAT Antibody, HRP conjugated

Code CSB-PA013069LB01HU
Size US$166
Order now
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) LRAT Polyclonal antibody
Uniprot No.
Target Names
LRAT
Alternative Names
LRAT; Lecithin retinol acyltransferase; Phosphatidylcholine--retinol O-acyltransferase
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Lecithin retinol acyltransferase protein (24-182AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
HRP
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (Probable). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology.
Gene References into Functions
  1. 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 PMID: 28942093
  2. 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. PMID: 28758396
  3. LRAT hypermethylation was associated with decreased mRNA levels in colorectal cancer clinical specimens. PMID: 25260806
  4. lecithin retinol acyltransferase affects all-trans retinoic acid levels and has a role in retinoid sensitivity in malignant melanoma cells. PMID: 25236354
  5. These findings reveal structural adaptation that facilitates selective catalysis and mechanism responsible for diverse substrate specificity within the LRAT-like enzyme family PMID: 25383759
  6. 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 PMID: 24433184
  7. 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. PMID: 23890161
  8. Lecithin-retinol acyltransferase is a thermostable and highly active enzyme with a likely mode of interfacial activation. PMID: 24613493
  9. A genetic defect was identified in LRAT as a novel cause of retinitis punctata albescens. PMID: 22559933
  10. Data show that acyl-modified forms of HRAS-like tumor suppressors HRASLS2 and HRASLS3 mimicking lipolytic activity of lecithin retinol acyltransferase LRAT. PMID: 22605381
  11. LRAT mutations cause a severe, early childhood onset, progressive retinal dystrophy. PMID: 22570351
  12. 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. PMID: 21465477
  13. Data show that overexpression of human LRAT specifically in mice oral basal epithelial cells makes these cells more sensitive to carcinogen induced tumorigenesis. PMID: 19471114
  14. LRAT expression is higher in renal tumors with an indolent biological behavior PMID: 14581364
  15. 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. PMID: 14596594
  16. LRAT has a role in preventing progression of invasive bladder cancer PMID: 15161698
  17. 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. PMID: 15474300
  18. LRAT has a role in retinoid absorption and storage PMID: 16115871
  19. These experiments are consistent with an expanded role for LRAT function as a protein palmitoyl transferase. PMID: 16939223
  20. The phenotype of patients with mutations in LRAT is similar to that of patients with mutations in RPE65, suggesting the need to systematically screen both genes in case of typical phenotype. PMID: 17011878
  21. LRAT mutations are likely a rare cause of Leber congenital amaurosis among patients from North America. PMID: 17438524
  22. Lecithin: retinol acyltransferase protein is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver. PMID: 18544127
  23. transcriptional regulation is aberrant in human prostate cancer and involves GATA transcription factors in normal prostate epithelial cells PMID: 18652909
  24. proximal region together with basal transcription factors may be sufficient to drive Lrat expression. PMID: 19665987

Show More

Hide All

Involvement in disease
Leber congenital amaurosis 14 (LCA14)
Subcellular Location
Endoplasmic reticulum membrane; Single-pass membrane protein. Rough endoplasmic reticulum. Endosome, multivesicular body. Cytoplasm, perinuclear region.
Protein Families
H-rev107 family
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
Database Links

HGNC: 6685

OMIM: 604863

KEGG: hsa:9227

STRING: 9606.ENSP00000337224

UniGene: Hs.658427

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
webinars: DT3C facilitates antibody internalization X
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*