Cleaved-Factor XII HC (I20) Polyclonal Antibody

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F12 encodes coagulation factor XII which circulates in blood as a zymogen. 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.

Synthesized peptide derived from the N-terminal region of human Factor XII HC at AA rangle: 10-90

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen

Cleaved-Factor XII HC (I20) Polyclonal Antibody detects endogenous levels of fragment of activated Factor XII HC protein resulting from cleavage adjacent to I20.