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This single chain zymogen is converted to a two-chain serine protease with an heavy chain (alpha-factor XIIa) and a light chain. The heavy chain contains two fibronectin-type domains, two epidermal growth factor (EGF)-like domains, a kringle domain and a proline-rich domain, whereas the light chain contains only a catalytic domain. On activation, further cleavages takes place in the heavy chain, resulting in the production of beta-factor XIIa light chain and the alpha-factor XIIa light chain becomes beta-factor XIIa heavy chain. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. The active factor XIIa participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. It activates coagulation factors VII and XI. Defects in this gene do not cause any clinical symptoms and the sole effect is that whole-blood clotting time is prolonged.
beta-factor XIIa part 1; Beta-factor XIIa part 2; coagulation factor XII; coagulation factor XII (Hageman factor); coagulation factor XIIa heavy chain; Coagulation factor XIIa light chain; F12; F13; Factor 12; factor XII; Factor12; FXII; HAE3; HAEX; HAF; hageman factor
150 µL
150 µL
100 µL
100 µL
100 µL
100 µg
100 µg
100 µg
100 µg
100 µL
100 µL
150 µL
1 mg
100 µL
1 mL
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