|Other Names||Coagulation factor XII, Hageman factor, HAF, Coagulation factor XIIa heavy chain, Beta-factor XIIa part 1, Beta-factor XIIa part 2, Coagulation factor XIIa light chain, F12|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta- factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa.|
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Provided below are standard protocols that you may find useful for product applications.
This gene 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.
Houlihan, L.M., et al. Am. J. Hum. Genet. 86(4):626-631(2010) Calafell, F., et al. Hum. Mol. Genet. 19(3):517-525(2010) Katakami, N., et al. Diabetes Care 33(2):390-395(2010) Back, J., et al. Biochem. Biophys. Res. Commun. 391(1):11-17(2010) Joseph, K., et al. Ann. Allergy Asthma Immunol. 104(1):50-54(2010) Bunkenborg, J., et al. Proteomics 4(2):454-465(2004) Hiller, O., et al. J. Biol. Chem. 275(42):33008-33013(2000)
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