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F10 undergoes multiple processing steps before its preproprotein is converted to a mature two-chain form by the excision of the tripeptide RKR. Two chains of the factor are held together by 1 or more disulfide bonds; the light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. The mature factor is activated by the cleavage of the activation peptide by factor IXa (in the intrisic pathway), or by factor VIIa (in the extrinsic pathway). The activated factor then converts prothrombin to thrombin in the presence of factor Va, Ca+2, and phospholipid during blood clotting. Mutations of this gene result in factor X deficiency, a hemorrhagic condition of variable severity.
Activated factor Xa heavy chain; blood coagulation factor X; Cf10; coagulation factor 10; coagulation factor X; coagulation factor X protein; F10; Factor 10; Factor X heavy chain; Factor X light chain; factor Xa; Factor10; FX; FXA; prothrombinase; RP11-98F14.9; stuart factor; Stuart-Prower factor; Unknown (protein for IMAGE:8121240); unnamed protein product
100 µL
150 µL
100 µg
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