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Key Documents

T7326

Sigma-Aldrich

Thrombin from bovine plasma

≥60 NIH units/mg protein (biuret)

Synonym(s):

Factor IIa

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥60 NIH units/mg protein (biuret)

composition

Protein, ≥50%

storage temp.

−20°C

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General description

Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Thrombin comprises of A-chain and B-chain with the catalytic pocket. The C-terminal regions has a fibrinogen recognition site (FRS) and a heparin binding site (HBS). The main function of thrombin is cleavage of fibrinogen to fibrin. It coordinates the coagulation cascade and coordinates with protease-activated receptors (PARs) to regulate physiological functions. High levels of thrombin causes neurotoxicity in dopaminergic neurons and contribute to the progression of parkinsons disease. Altered thrombin levels modulates coagulation pathway in multiple sclerosis. Patients with coronary artery disease (CAD) show elevated levels of thrombin.

Application

Thrombin from bovine plasma may be used:
  • for the generation of fibrin from fibrinogen embedded in microbubbles
  • for the cleavage of hydrogenase maturation protein (HypF-N) from the nickel resin

as revitalization model to mimic blood fabrication in root canal
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 evaluate coagulation abnormalities in acute liver failure.

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.

Physical form

Lyophilized powder containing sodium chloride and Tris-HCl, pH 7.0

Preparation Note

Traditional thrombin products are activated with bovine brain thromboplastin, whereas T7326 is activated with bovine lung thromboplastin and does not contain any bovine brain products in its preparation.

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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Increased plasma thrombin potential is associated with stable coronary artery disease: An angiographically-controlled study
Tosi F, et al.
Thrombosis Research, 155, 16-22 (2017)
Banwari Agarwal et al.
Journal of hepatology, 57(4), 780-786 (2012-06-28)
In acute liver failure (ALF), prothrombin time (PT) and its derivative prothrombin time ratio (PTR) are elevated, and are considered predictors of increased bleeding risk. We aimed at determining whether increased PT/PTR reflects the haemostatic potential and bleeding risk in
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers
Patel JR, et al.
Biomolecular NMR Assignments, 1-5 (2018)
A training model for revitalization procedures
Widbiller M, et al.
International Endodontic Journal, 51, e301-e308 (2018)
Fibrin-Targeted Polymerized Shell Microbubbles as Potential Theranostic Agents for Surgical Adhesions
Gormley CA, et al.
Langmuir (2019)

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