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  • F8396 - Monoclonal Anti-Factor X antibody produced in mouse

F8396 Sigma

Monoclonal Anti-Factor X antibody produced in mouse

clone HX-1, purified immunoglobulin, buffered aqueous solution



Related Categories Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies for Immune Cell Signaling and Blood, Antibodies to Clotting Factors,
species reactivity   human
application(s)   western blot: 0.125-0.25 μg/mL
clone   HX-1, monoclonal
concentration   ~1 mg/mL
antibody form   purified immunoglobulin
form   buffered aqueous solution
isotype   IgG2b
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... F10(2159)
biological source   mouse
conjugate   unconjugated



Factor X from pooled normal human plasma

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.

Physical form

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


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


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

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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.

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Safety Information

WGK Germany  3
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