Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SERPINE2 in samples. An antibody specific for SERPINE2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySERPINE2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SERPINE2 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 SERPINE2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Protease nexin I is a 44-kD thrombin and urokinase inhibitor released by human foreskin fibroblasts. PN-I shares several features with antithrombin III , an abundant plasma thrombin inhibitor. Both PN-I and AT-III have high affinities for heparin, and heparin accelerates their rate of thrombin inhibition. In addition, the published sequence of 28 amino acids at the N-terminus of PN-I is identical to the N-terminal amino acid sequence of a glial-derived neurite promoting factor. Two forms, designated alpha and beta, were identified. These differed only by the insertion of 3 nucleotides into the coding sequence, and apparently arose by utilization of an alternative splice acceptor site in the PN1 gene. In the resulting proteins, alpha-PN-I contains an arginine residue at position 310, whereas beta-PN-I contains threonine-lysine residues.
