Application

Monoclonal Anti-Factor X antibody is suitable for western blot at 0.125-0.25 ug/mL.

Biochem/physiol Actions

The peptide bond cleavage in the heavy chain triggers the activity of factor X zymogen and clips off a carbohydrate rich peptide. Factor X activity can also be accelerated by a protease from Russell′s viper venom. Upon activation, it catalyzes the conversion of prothrombin to thrombin. It cleaves two peptide bonds of prothrombin by binding to the Factor Va and a phospholipid on cell surfaces in presence of calcium ions.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Factor X is the vitamin K-dependent pro-coagulants with molecular weight of 68,000. It is synthesized in the liver and consists of a heavy chain and a light chain which are linked by a disulfide bond. The primary domain present in the light chain contains 11 γ-carboxy glutamic acid residues at the N-terminal end. The N-terminal primary domain is responsible for binding of negatively charged phospholipids. Primary domain of the heavy chain present at the C-terminal end has similar characteristics with the serine proteases.

Immunogen

Factor X from pooled normal human plasma

Physical form

Solution in 10 mM HEPES, pH 7.4, with 140 mM sodium chloride and 0.05% sodium azide

Specificity

Monoclonal Anti-Factor X, a divalent cation-independent antibody, recognizes an epitope on the light chain of human Factor X (~68 kDa) and active Factor Xa (~55 kDa), This antibody inhibits the activity of Factor X