Minami et al. (1987) reported the full-length cDNA and complete primary structure of human LTA4 hydrolase. This was the first report of the molecular cloning of an enzyme involved in the biosynthesis of eicosanoids. Funk et al. (1987) isolated a cDNA clone corresponding to leukotriene A4 hydrolase from a human lung lambda-gt11 expression library by immunoscreening with a polyclonal antiserum. Several additional clones from human lung and placenta cDNA lambda-gt11 libraries were obtained by plaque hybridization with the (32)P-labeled lung cDNA clone. One of the clones had an insert of 1,910 basepairs that contained a complete protein-coding region. From the deduced primary structure, leukotriene A4 hydrolase is a 610-amino acid protein with a calculated molecular weight of 69,140.

Human Leukotriene A-4 hydrolase (LTA4H) ELISA Kit employs a two-site sandwich ELISA to quantitate LTA4H in samples. An antibody specific for LTA4H has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyLTA4H present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for LTA4H is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of LTA4H bound in the initial step. The color development is stopped and the intensity of the color is measured.

Human Leukotriene A-4 hydrolase (LTA4H) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.

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