Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate F13B in samples. An antibody specific for F13B has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyF13B present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for F13B 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 F13B bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as a plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon activation by the cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot.
