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Overview
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Background
After proteolytic activation by thrombin, FXIIIa modifies the soft fibrin clot and thereby introducing covalent bonds. First, cross-linking between abutting γ-chains of fibrin is catalyzed and subsequently α2-antiplasmin is incorporated to further increase the resistance against fibrinolysis. Plasmin catalyses the retarded clot dissolution and the release of crosslinked fibrin degradation products (xFDPs / D-dimer). Monoclonal “D-dimer” antibodies (e.g. DD-3B6/22) are commercially available and are used in In Vitro Diagnostics (IVD) to exclude thromboembolic events. However, these monoclonals do not detect the crosslink itself but address a portion of polypeptides within the D-domain after plasmin degradation that are conformationally reactive. Zedira scientists developed a monoclonal antibody which directly recognizes the crosslinked fibrin neoepitope (DD-XLink-mab).For more information klick here: Poster presentation at GRC, 2016 (Girona, Spain)
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