F8396
Monoclonal Anti-Factor X antibody produced in mouse
clone HX-1, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Anti-FX
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About This Item
Recommended Products
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
HX-1, monoclonal
form
buffered aqueous solution
species reactivity
human
concentration
~1 mg/mL
technique(s)
western blot: 0.125-0.25 μg/mL
isotype
IgG2b
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... F10(2159)
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.
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
Immunogen
Factor X from pooled normal human plasma
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.
Physical form
Solution in 10 mM HEPES, pH 7.4, with 140 mM sodium chloride and 0.05% sodium azide
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.
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Storage Class
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Activation of human factor X (Stuart factor) by a protease from Russell's viper venom.
R G Di Scipio et al.
Biochemistry, 16(24), 5253-5260 (1977-11-29)
The conversion of prothrombin to thrombin. III. The factor Xa-catalyzed activation of prothrombin.
C T Esmon et al.
The Journal of biological chemistry, 249(24), 7782-7790 (1974-12-25)
Simon N Waddington et al.
Cell, 132(3), 397-409 (2008-02-13)
Adenoviruses are used extensively as gene transfer agents, both experimentally and clinically. However, targeting of liver cells by adenoviruses compromises their potential efficacy. In cell culture, the adenovirus serotype 5 fiber protein engages the coxsackievirus and adenovirus receptor (CAR) to
The role of serine proteases in the blood coagulation cascade.
E W Davie et al.
Advances in enzymology and related areas of molecular biology, 48, 277-318 (1979-01-01)
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