T4393
Thrombine from human plasma
lyophilized powder, 1500-3500 NIH units/mg protein (E1%/280, 18.3), suitable for cell culture
Synonyme(s) :
Facteur IIa
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About This Item
Produits recommandés
Source biologique
human plasma
Niveau de qualité
Stérilité
sterile
Forme
lyophilized powder
Activité spécifique
1500-3500 NIH units/mg protein (E1%/280, 18.3)
Technique(s)
cell culture | mammalian: suitable
Impuretés
HIV, hepatitis B and hepatitis C, tested negative
Numéro d'accès UniProt
Température de stockage
−20°C
Informations sur le gène
human ... F2(2147)
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Description générale
Thrombin is produced from the proteolytic cleavage of inactive prothrombin in the liver. The prothrombin gene is mapped to human chromosome 11p11.2. It comprises of A and B catalytic domain, recognition domain and insertion loops. The active site residues comprise the catalytic tetrad, (histidine 57, aspartate 102, serine 195 and serine 214).
Application
Thrombin from human plasma has been used:
- as a medium supplement for the pre-treatment of endothelial cell culture prior to confocal microscopy and enzyme linked immunosorbent assay (ELISA)
- in the gelatinization of mesenchymal stem cells (MSCs) for preparing fibrin–MSC construct
- for screening serine protease inhibitor, OGTI from frog skin secretion
Actions biochimiques/physiologiques
The main function of thrombin is the cleavage of fibrinogen to fibrin, to assist stable clot formation. High levels of thrombin elicit neurotoxicity in dopaminergic neurons and contributes to the progression of Parkinson′s disease. A wide range of mutations in the prothrombin gene contributes to its deficiency resulting in coagulation disorders like dysprothrombinemia and hypoprothrombinemia. Altered thrombin levels modulates the coagulation pathway in multiple sclerosis. Patients with coronary artery disease (CAD) show elevated levels of thrombin. Thrombin accumulation in neurofibrillary tangles in the brain may contribute to the aggregation of τ protein and pathophysiology of Alzheimer disease.
Sérine protéase qui clive sélectivement les liaisons Arg-Gly du fibrinogène pour former la fibrine et les fibrinopeptides A et B.
Définition de l'unité
Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard
Reconstitution
When reconstituted with 1 mL water, vial contains stated activity in 0.15 M sodium chloride and 0.05 M sodium citrate, pH 6.5.
Remarque sur l'analyse
The NIH assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of Biggs. Only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations.
Clause de non-responsabilité
Ce produit, destiné à la recherche scientifique, est soumis à une réglementation spécifique en France, y compris pour les activités d′importation et d′exportation (Article L 1211-1 alinéa 2 du Code de la Santé Publique). L′acheteur (c′est-à-dire l′utilisateur FINAL) est tenu d′obtenir une autorisation d′importation auprès du ministère français de la recherche, mentionné à l′article L1245-5-1 II du Code de la Santé Publique. En commandant ce produit, vous confirmez détenir l′autorisation d′importation requise.
Inhibiteur
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
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Thrombin generation correlates with disease duration in multiple sclerosis (MS): Novel insights into the MS-associated prothrombotic state
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Multiple Sclerosis Journal, 3(4) (2017)
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Shovlin CL, et al.
PLoS ONE, 5(2), e9154-e9154 (2010)
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Richard C Rogers et al.
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Articles
Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.
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