Sheep Anti-Human Fibrin Fragment E polyclonal antibody for IEP, ELISA. Fibrinogen is an abundant plasma protein (5-10 µM) produced in the liver. The intact protein has a molecular weight of 340 kDa and is composed of 3 pairs of disulphide-bound polypeptide chains named A?, B? and ?. Fibrinogen is a triglobular protein consisting of a central E domain and terminal D domains. Proteolysis by thrombin results in release of Fibrinopeptide A (FPA, A?1-16) followed by Fibrinopeptide B (FPB, B?1-14) 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 ?, ? and ?, 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 ? chains and, to a lesser extent, ? chains of the fibrin molecules. Proteolysis of fibrinogen by plasmin initially liberates Cterminal residues from the A? chain to produce fragment X (intact DE-D, which is still clottable). Fragment X is further degraded to nonclottable fragments Y (D-E) and D. Fragment Y can be digested into its constituent D and E fragments. Digestion of non-crosslinked fibrin with plasmin is very similar to the digestion of fibrinogen, which results in production of fragments D and E. Degradation of crosslinked fibrin by plasmin results in fragment DD (D-Dimer consisting of the D domains of 2 fibrin molecules crosslinked via the ? chains), fragment E (central E domain) as well as DDE in which fragment E is non-covalently associated with DD. For human crosslinked fibrin, the relative weights of the cleavage fragments produced are: 184 kDa for fragment DD, 92 kDa for D, 50 kDa for E, 1.54 kDa for FPA and 1.57 kDa for FPB.
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