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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-648-7
MDL number:
form
lyophilized powder
specific activity
40-300 NIH units/mg protein (biuret)
composition
Protein, 40-60%
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... F2(280685)
General description
Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Lyophilized powder containing sucrose, sodium chloride and Tris.
Application
Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to assess characterization of platelet dysfunction after trauma.
Biochem/physiol Actions
Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.
Physical form
Lyophilized powder containing sodium chloride and Tris-HCl, pH 7.0
Preparation Note
Prepared using bovine lung thromboplastin for conversion to the active form.
Analysis Note
Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard, Lot K.
The NIH assay procedure uses 0.2 mL of diluted plasma (1:1 with saline) as a substrate and 0.1 mL 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.
Other Notes
View more information on thrombin at www.sigma-aldrich.com/enzymeexplorer.
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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 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Related Content
Instructions
Matthew E Kutcher et al.
The journal of trauma and acute care surgery, 73(1), 13-19 (2012-06-30)
The increased morbidity and mortality associated with coagulopathy and thrombocytopenia after trauma are well described. However, few studies have assessed platelet function after injury. Blood samples were prospectively collected from 101 patients with critical injury and trauma on arrival to
Hans P Kohler
Blood, 121(11), 1931-1932 (2013-03-16)
In this issue of Blood, Smith and colleagues report on the functional role of the interaction between these 2 proteins by studying the involved binding sites responsible for clot stabilization.(1)
Stephen R Clark et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(15), 5875-5880 (2013-03-27)
Aminophospholipid (APL) trafficking across the plasma membrane is a key event in cell activation, apoptosis, and aging and is required for clearance of dying cells and coagulation. Currently the phospholipid molecular species externalized are unknown. Using a lipidomic method, we

