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F8396

Sigma-Aldrich

Monoclonal Anti-Factor X antibody produced in mouse

clone HX-1, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Anti-FX

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About This Item

Numéro MDL:
MFCD00164644
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

HX-1, monoclonal

Forme

buffered aqueous solution

Espèces réactives

human

Concentration

~1 mg/mL

Technique(s)

western blot: 0.125-0.25 μg/mL

Isotype

IgG2b

Numéro d'accès UniProt

P00742

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... F10(2159)

Description générale

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.

Spécificité

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

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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