Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate Fb in samples. An antibody specific for Fb has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyFb present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for Fb 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 Fb bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Fibrinogen is an abundant plasma protein (5-10uM) produced in the liver. The intact protein has a MW of 340kD. It is composed of 3 pairs of disulfide-bound polypeptide chains named Aalpha, Bbeta and gamma. Fibrinogen is a triglobular protein consisting of a central E domain and terminal D domains. Proteolysis by thrombin results in release of Fibrinopeptide A followed by Fibrinopeptide B and the fibrin monomers that result polymerize in a half-overlap fashion to form insoluble fibrin fibrils. The chains of fibrin are referred to as alpha, beta and gamma, due to the removal of FPA and FPB. The polymerised fibrin is subsequently stabilized by the transglutaminase activated Factor XIII that forms amide linkages between gamma chains and, to a lesser extent, alpha chains of the fibrin molecules. Proteolysis of fibrinogen by plasmin initially liberates C-terminal residues from the Aalpha chain to produce fragment X.