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biological source
bovine
Quality Level
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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
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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