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Merck
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Key Documents

604980

Sigma-Aldrich

Thrombin, Bovine, High Activity

Sinónimos:

Thrombin, Bovine, High Activity

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About This Item

Número de CAS:
9002-04-4
UNSPSC Code:
12352204
NACRES:
NA.25

biological source

bovine

Quality Level

100

form

lyophilized

specific activity

≥1800 NIH units/mg protein

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

solubility

water: soluble

shipped in

ambient

storage temp.

−20°C

General description

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

Biochem/physiol Actions

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.

Warning

Toxicity: Harmful (C)

Physical form

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

Analysis Note

Complete activation from homogeneous prothrombin by SDS-PAGE

Legal Information

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

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Kitchens CS, et al.
Consultative Hemostasis and Thrombosis null
Segall JA and Liem TK
Congenital and Acquired Hypercoagulable Syndromes, 339-346 (2007)
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
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
Dillon K Jarrell et al.
PloS one, 16(5), e0239242-e0239242 (2021-05-20)
Fibrin has been used clinically for wound coverings, surgical glues, and cell delivery because of its affordability, cytocompatibility, and ability to modulate angiogenesis and inflammation. However, its rapid degradation rate has limited its usefulness as a scaffold for 3D cell
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