epitope mapping within an internal region of LRAT of mouse origin
recommended for detection of LRAT of mouse and, to a lesser extent, rat origin by WB, IF and ELISA; also reactive with additional species, including porcine
TransCruz reagent for Gel Supershift and ChIP applications, sc-49222 X, 200 µg/0.1 ml
LRAT Background Information 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.
