Recombinant Mouse Lecithin retinol acyltransferase (Lrat), partial

Code CSB-YP862362MO
MSDS
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Source Yeast
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Code CSB-EP862362MO
MSDS
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Source E.coli
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Code CSB-EP862362MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP862362MO
MSDS
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Source Baculovirus
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Code CSB-MP862362MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Lrat
Uniprot No.
Alternative Names
Lrat; Lecithin retinol acyltransferase; EC 2.3.1.135; Phosphatidylcholine--retinol O-acyltransferase; Phosphatidylcholine-retinol-O-acyltransferase
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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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. LRAT plays a critical role in vision. 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. Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology.
Gene References into Functions
  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 PMID: 25317684
  2. LRAT overexpression diminishes intracellular levels of biologically active retinoids and reduces retinoid antitumor efficacy in the murine melanoma PMID: 25721651
  3. Mislocalized M-opsin was degraded whereas mislocalized S-opsin accumulated in Lrat(-/-) cones before the onset of massive ventral/central cone degeneration. PMID: 24664772
  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. PMID: 22637576
  5. Lrat KO mice exhibited increased levels of retinoic acid-responsive genes, including p21. PMID: 22116467
  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. PMID: 20628054
  7. FATP1 inhibits 11-cis retinol formation via interaction with the visual cycle retinoid isomerase RPE65 and lecithin:retinol acyltransferase PMID: 20356843
  8. 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
  9. Lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters in the eye and in the liver PMID: 14684738
  10. LRAT has a role in retinoid absorption and storage PMID: 16115871
  11. LRAT-/- mice are much more susceptible to vitamin A deficiency and should be an excellent animal model of vitamin A deficiency PMID: 16174770
  12. analysis of the topology and subcellular localization of LRAT, a critical enzyme in vitamin A metabolism PMID: 17114808
  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 PMID: 17504753
  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. PMID: 18055784
  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 PMID: 18093970
  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. PMID: 18296659
  17. proximal region together with basal transcription factors may be sufficient to drive Lrat expression. PMID: 19665987

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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).
Database Links
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