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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
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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. [1]

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

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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
Dabigatran: a nephrological way out.
Patricio A Pazmiño
The American journal of medicine, 126(4), e21-e21 (2013-03-20)
Pancras C Wong et al.
Hospital practice (1995), 41(1), 19-25 (2013-03-08)
The effect of the oral direct activated factor X (factor Xa) inhibitor apixaban on tissue factor-induced thrombin generation in human plasma was investigated in vitro using the calibrated automated thrombogram (CAT) method and compared with the oral direct factor Xa
Ildiko M Kovach et al.
Biochemistry, 52(14), 2472-2481 (2013-03-23)
Thrombin is the pivotal serine protease enzyme in the blood cascade system and thus a target of drug design for control of its activity. The most efficient nonphysiologic inhibitor of thrombin is hirudin, a naturally occurring small protein. Hirudin and
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

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