Description
Principle of the assay: This assay employs a two-site sandwich ELISA to quantitative PP13 in Human serum, plasma. An antibody specific for PP13 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any PP13 present is bound by the immobilized antibody. After removing any unbound substances, a biotin - conjugated antibody specific for PP13 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 PP13 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Background: Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. Galactoside-binding soluble lectin 13 has lysophospholipase activity. It is composed of two identical subunits which are held together by disulfide bonds. This protein has structural similarity to several members of the beta-galactoside-binding S-type lectin family. By ultracentrifugation and SDS-PAGE, LGALS13 showed an apparent molecular mass of 29 to 30 kD. Under reducing conditions, the apparent molecular mass was 16 kD, suggesting that LGALS13 is composed of 2 identical subunits held together by disulfide bonds. Western blot analysis and Ouchterlony gel diffusion were unable to detect LGALS13 in serum or in any other adult or fetal tissue examined