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About This Item
Specific activity:
≥1800 NIH units/mg protein
Biological source:
bovine
biological source
bovine
Quality Segment
description
Merck USA index - 14, 9383
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.
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
Disclaimer
Toxicity: Harmful (C)
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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