Human Peroxisome Proliferator-activated receptor Beta (PPAR-B) ELISA Kit

This assay employs a two-site sandwich ELISA to quantitate PPAR-B in Human serum, plasma. An antibody specific for PPAR-B has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any PPAR-B present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for PPAR-B 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 PPAR-B bound in the initial step. The color development is stopped and the intensity of the color is measured.

PPARb is only weakly activated by fatty acids, prostaglandins and leukotrienes and has no known physiologically relevant ligand. However, data from PPARb null mice suggest PPARb does serve a role in fatty acid metabolism and perhaps in skin proliferation and cancer. A role for the nuclear receptor peroxisome proliferator-activated receptor-b (PPARb) in oncogenesis has been suggested by a number of observations but its precise role remains elusive. Prostaglandin I2 (PGI2,prostacyclin), a major arachidonic acid (AA) derived cyclooxygenase (Cox) product, has been proposed as a PPARb agonist. Surprisingly, however, 4-OHT failed to activate PPARb transcriptional activity,indicating that PGI2 is insufficient for PPARb activation. Conversely, inhibition of PGIS blocked PGI2 synthesis but did not affect the AA mediated activation of PPARb.