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Key Documents

F8396

Sigma-Aldrich

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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

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 Code

10 - Combustible liquids

WGK

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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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
Kathrin Becker et al.
Frontiers in immunology, 12, 640842-640842 (2021-04-30)
Neutrophil extracellular traps (NETs) have been identified as one pathogenetic trigger in severe COVID-19 cases and therefore well-described animal models to understand the influence of NETs in COVID-19 pathogenesis are needed. SARS-CoV-2 infection causes infection and interstitial pneumonia of varying
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 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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