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F8396

Sigma-Aldrich

Monoclonal Anti-Factor X antibody produced in mouse

clone HX-1, purified immunoglobulin, buffered aqueous solution

Sinonimo/i:

Anti-FX

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

HX-1, monoclonal

Forma fisica

buffered aqueous solution

Reattività contro le specie

human

Concentrazione

~1 mg/mL

tecniche

western blot: 0.125-0.25 μg/mL

Isotipo

IgG2b

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... F10(2159)

Descrizione generale

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.

Specificità

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

Immunogeno

Factor X from pooled normal human plasma

Applicazioni

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

Azioni biochim/fisiol

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.

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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)
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)
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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