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|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic peptide derived from the internal region of human LRAT|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.4, with 50% glycerol, 150mM NaCl|
|Contains||0.02% sodium azide|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:100|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Lecithin retinol acyltransferase (LRAT) is a membrane bound enzyme that catalyzes the transfer of an acyl group from the sn-1 position of lecithin to vitamin A which generates all-trans-retinyl esters (tREs) in the liver, some extrahepatic tissues, such as the lung, and retinal pigmented epithelium. LRAT can also exchange palmitoyl groups between RPE65, a tRE binding protein essential for vision, and tREs, which is important for the operation of the visual pathway. LRAT is essential for the dietary mobilization, transport, and storage of vitamin A as well as the synthesis of the visual pigment chromophore. LRAT monomers interact in membranes to form homodimers through disulfide bond formation. A loss of LRAT correlates with an early onset severe retinal dystrophy and severe retinyl ester deprivation, while a reduction in LRAT expression may be associated with invasive bladder cancer.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Lecithin retinol acyltransferase; lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase); Phosphatidylcholine--retinol O-acyltransferase; Phosphatidylcholine-retinol O-acyltransferase; Phosphatidylcholine-retinol-O-acyltransferase
1300010A18Rik; AI449251; LCA14; LRAT