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T6200

Sigma-Aldrich

Thrombin from bovine plasma

lyophilized powder, 40-300 NIH units/mg protein (biuret)

Synonym(s):

Factor IIa

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204

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)

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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.

pictograms

Health hazardExclamation mark

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 2

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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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
The reply.
Peter R Kowey et al.
The American journal of medicine, 126(4), e23-e23 (2013-03-20)
Response.
Sarah T Garber et al.
Journal of neurosurgery, 118(2), 485-485 (2013-03-16)

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