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