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Key Documents

T4393

Sigma-Aldrich

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

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.75

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.

Pictogrammes

Health hazard

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)

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

A small trypsin inhibitor from the frog of Odorrana grahami
Li J, et al.
Biochimie, 90(9), 1356-1361 (2008)
Endothelial cell processing and alternatively spliced transcripts of factor VIII: potential implications for coagulation cascades and pulmonary hypertension
Shovlin CL, et al.
PLoS ONE, 5(2), e9154-e9154 (2010)
Richard C Rogers et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 318(6), R1068-R1077 (2020-04-23)
Severe trauma can produce a postinjury "metabolic self-destruction" characterized by catabolic metabolism and hyperglycemia. The severity of the hyperglycemia is highly correlated with posttrauma morbidity and mortality. Although no mechanism has been posited to connect severe trauma with a loss
Thrombin generation correlates with disease duration in multiple sclerosis (MS): Novel insights into the MS-associated prothrombotic state
Parsons MEM, et al.
Multiple Sclerosis Journal, 3(4) (2017)
Chia-Chun Chen et al.
Journal of orthopaedic research : official publication of the Orthopaedic Research Society, 30(3), 393-400 (2012-01-24)
Extracellular matrix (ECM) is thought to participate significantly in guiding the differentiation process of mesenchymal stem cells (MSCs). In this study, we hypothesized that cartilage fragments from osteoarthritic knee could promote chondrogenesis of MSCs. Nonworn parts of cartilage tissues were

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.

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.

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.

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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