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Merck
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Key Documents

604980

Sigma-Aldrich

Thrombin, Bovine, High Activity

Synonyme(s) :

Thrombin, Bovine, High Activity

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About This Item

Numéro CAS:
9002-04-4
Code UNSPSC :
12352204

Source biologique

bovine

Niveau de qualité

100

Forme

lyophilized

Activité spécifique

≥1800 NIH units/mg protein

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Solubilité

water: soluble

Conditions d'expédition

ambient

Température de stockage

−20°C

Description générale

Thrombin is a sodium-activated type II enzyme. This serine protease enzyme consists of two anion binding exosites, ABE-I and ABE-II. Thrombin is synthesized from zymogen prothrombin (factor II) in the liver. Bovine A-thrombin comprises a light chain (A chain) and a heavy chain (B chain). These two chains are linked by non-covalent interactions and by one disulfide bond.

Application

Thrombin, bovine, high activity has been used:
  • to stimulate LNCaP cell and to study the effect of activation of G-protein-coupled receptors (GPCRs)
  • in fibrin gel fabrication
  • to form fibrinogen gel by fibrinogen gel-based method

Actions biochimiques/physiologiques

Thrombin converts fibrinogen into fibrin and activates factors V, VIII, XI, and XIII. It promotes platelet activation and vascular contraction. Thrombin stabilizes the fibrin polymers. It plays a crucial role in the final stages of the blood coagulation cascade.

Avertissement

Toxicity: Harmful (C)

Forme physique

Lyophilized from 200 mM NaCl, 50 mM sodium citrate, 1 ml 0.1% PEG, pH 6.5.

Remarque sur l'analyse

Complete activation from homogeneous prothrombin by SDS-PAGE

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictogrammes

Exclamation markHealth hazard
GHS07,GHS08

Mention d'avertissement

Danger

Mentions de danger

H315 - H319 - H334 - H335

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

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

Kitchens CS, et al.
Consultative Hemostasis and Thrombosis null
Segall JA and Liem TK
Congenital and Acquired Hypercoagulable Syndromes, 339-346 (2007)
Diana L Diesen et al.
Vascular, 16 Suppl 1, S29-S36 (2008-03-01)
Thrombin is a common hemostatic drug used in surgical practice for over 100 years because of its simplicity and efficacy. Thrombin converts fibrinogen to fibrin, activates platelets, and induces vascular contraction. It is available in multiple forms, including human thrombin
Isis S R Carter et al.
Thrombosis, 2010, 416167-416167 (2010-01-01)
Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region
Li Xiao et al.
Antioxidants (Basel, Switzerland), 10(1) (2021-01-13)
Ultraviolet-A (UVA) irradiation induces harmful effects on skin cells and accelerates skin aging through oxidative stress. In this study, the effects of a hydrogen-generating silica material named ULH-002 against UVA injuries in human cells and 3D skin equivalents were investigated.
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