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T7572

Sigma-Aldrich

Thrombin from human plasma

400-1000 NIH units/mg protein

Synonym(s):

Factor IIa

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About This Item

CAS Number:
9002-04-4
Enzyme Commission number:
3.4.21.5 (BRENDA, IUBMB)
EC Number:
232-648-7
MDL number:
MFCD00082072
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

200

specific activity

400-1000 NIH units/mg protein

impurities

HIV, hepatitis B and hepatitis C, tested negative

UniProt accession no.

P00734

storage temp.

−20°C

Gene Information

human ... F2(2147)

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General description

Lyophilized powder containing sucrose, sodium chloride and Tris.
Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.

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 an innovative flow cytometric approach for small-size platelet microparticles.

Biochem/physiol Actions

Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.

Unit Definition

Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard

Analysis Note

The NIH assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1ml 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.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

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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Silvia Montoro-García et al.
Thrombosis and haemostasis, 108(2), 373-383 (2012-06-29)
Microparticles (MPs) are small submicron membrane-derived vesicles shed from a variety of cells and they have been implicated in different disorders. Accordingly, understanding of physiological characteristics of MPs and improvement of methods of their quantification are important for further advance
At the cutting edge: conformational PARtiality.
T Madhusudhan et al.
Journal of thrombosis and haemostasis : JTH, 10(8), 1672-1674 (2012-06-30)
Herbert Nar
Trends in pharmacological sciences, 33(5), 279-288 (2012-04-17)
The quest for novel medications to treat thromboembolic disorders such as venous thrombosis, pulmonary embolism and stroke received a boost when the 3D structures of two major players in the blood coagulation cascade were determined in 1989 and 1993. Structure-guided
Jawed Fareed et al.
Annual review of pharmacology and toxicology, 52, 79-99 (2011-08-09)
Since the discovery of heparin nearly a century ago, there have been large gaps in the development of anticoagulants. The discovery of warfarin was the first step toward using oral anticoagulants, but warfarin use has been associated with its own
Christopher S King et al.
Chest, 143(4), 1106-1116 (2013-04-03)
Thromboembolic diseases are common. Heparins and the vitamin K antagonists have been the mainstay of therapy for > 60 years, but both classes of agents have limitations. The "ideal" anticoagulant should be as effective and safe as heparin and vitamin
View All Related Papers

Articles

Thrombin Factor IIa

Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

Thrombin Factor IIa

Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

Thrombin Factor IIa

Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

Thrombin Factor IIa

Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

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