Factor II (FII) is a glycoprotein synthesized by the liver, zymogen of a serine protease. It is a vitamin K-dependent clotting factor. Its half-life is 50 to 120 hours.
FII is activated by the prothrombinase thrombin complex which plays a central role in the coagulation process.
It will transform fibrinogen into fibrin, amplify its own formation and activate the protein C, TAFI and platelet systems.
There are constitutional deficits in FII which are very rare and acquired deficits which can be observed during anti-vitamin K treatment or vitamin K deficiency, CIVD, anti-FII autoantibodies.
FII insufficiency as well as replacement therapy for FII can be monitored. (Specialized hemostasis)
The functional activity of FII is determined by the enzymatic method of chromogenic prothrombinase in which human FII is activated to thrombin (IIa) by FXa in the presence of bovine FV, phospholipids and calcium ions.
The amount of FIIa thus generated is determined by the hydrolysis of a chromogenic substrate of FIIa.
The FII activity of the sample is determined against a concentrated or plasma standard and the result is expressed in International Units (IU).
- Excellent sensitivity around 0.25 mIU / mL unaffected by hemoglobin, bilirubin, triglycerides / heparins (UFH & LMWH)
- Based on prothrombinase complex to reflect biological activity
- Significant dilution of the sample which limits the generation of thrombin
- Very robust dosage because complete activation of prothrombin
- The biologically inactive prothrombin precursor (DCP) is not activated in this method.
- 4 vials x activator reagent (human FXa, bovine FVa, CaCl2, phospholipids) (3 mL)
- 1 vial x chromogenic substrate (6 mL)
- 1 vial x dilution buffer (20 mL)
