F8396
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
Produits recommandés
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
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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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)
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
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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