Factor X is a vitamin K dependant, two-chain glycoprotein zymogen (Mr = 59 000) synthesized in the liver that circulates in plasma at a concentration of approximately 10 μg/mL.
Activation to factor Xa occurs by interaction with the intrinsic factor Xase complex (factor VIIa / IXa / Ca2+ / phospholipid) or the extrinsic factor Xase complex (Factor VIIa/tissue factor/Ca2+/phospholipid). Both complexes cleave the molecule at Arg52-Ile53, release an activation peptide from the heavy chain, resulting in factor Xa as a two-chain molecule where the light chain remains with a Mr of 17 000 and the heavy chain has been reduced to a Mr of 29 000.
Factor Xa provides the enzymatic activity of the prothrombinase complex (factor Xa / Factor Va / Ca2+ / phospholipid) which converts prothrombin to thrombin. While FXa can convert prothrombin to thrombin alone, its activity is greatly enhanced when a part of the complex. Its activity may be inhibited by inactivation of the factor Va cofactor or directly by a natural inhibitor such as antithrombin III (ATIII).
Screw-capped glass vial containing 80 μg of human factor Xa lyophilized.
All enzymes are accompanied by certificates of analysis which describe the appropriate storage conditions.
In order for us to guarantee the stability of the product, it is imperative that the storage conditions are observed.
The lyophilized presentation allows greater stability until the expiration date.
