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Description
Sheep Anti-Human Factor XIII polyclonal antibody for IEP, ELISA. Factor XIII (F.XIII, fibrin stabilizing factor) is the proenzyme form of a transamidase that is essential for normal haemostasis and fibrinolysis, wound healing, female fertility and foetal development. Extracellular F.XIII consists of A subunits (83 kDa each) which contain the enzyme moiety, and B subunits (76 kDa each) which act as a carrier protein for the A subunit in circulation. Both subunits are produced under separate genetic control. In plasma, F.XIII exists as a non-covalent tetrameric complex (320 kDa) of two A-subunits and two B-subunits (A2B2). The concentration of F.XIII tetramer in plasma is ~25 μg/ml (~80 nM). An intracellular form of F.XIII is found in platelets, megakaryocytes and monocytes. This form of F.XIII presents as a dimer of two A-subunits only and has a molecular weight of 160 kDa. The importance of these intracellular stores is demonstrated by the observation that platelets can contribute up to half of the F.XIII activity in platelet rich plasma. The activation of F.XIII involves several steps. Thrombin cleaves after Arg37 of each A-subunit in the A2B2 tetramer, releasing a 4.5 kDa activation peptide. Additional conformational changes induced by the binding of calcium, and by dissociation of the B-subunits from the A-subunit dimer are required to obtain full enzyme activity. F.XIIIa is a cysteine protease that catalyses the formation of β-glutamyl-ε-lysyl bonds between the β and α chains of polymerised fibrin molecules. Other proteins found crosslinked into fibrin clots by F.XIIIa include fibrinogen, α2 Antiplasmin, fibronectin, vitronectin and von Willebrand factor.