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T6884 Sigma-Aldrich

Thrombin from human plasma

lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280, 18.3)

Synonym: Factor IIa

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Description

General description

Thrombin is produced from the proteolytic cleavage of inactive prothrombin in the liver. It is a glycoprotein with four structural domains: the 10 γ-carboxylated glutamic acid containing Gal domain, two kringle domains, and the trypsin-like serine protease domain. The prothrombin gene is mapped to human chromosome 11p11.2.

Application

Thrombin from human plasma has been used:
• in the preparation of fibrin gels for assessing human bone marrow stromal cells (hBMSC) morphology,
• in the activation of platelets,
• to evaluate the integrity of endothelial cell (EC) monolayers

Biochem/physiol Actions

The main function of thrombin is the cleavage of fibrinogen to fibrin, to assist stable clot formation. A wide range of mutations in the prothrombin gene contributes to its deficiency resulting in coagulation disorders like dysprothrombinemia and hypoprothrombinemia. High levels of thrombin elicit neurotoxicity in dopaminergic neurons and contributes to the progression of Parkinson′s disease. Altered thrombin levels modulates the coagulation pathway in multiple sclerosis. Patients with coronary artery disease (CAD) show elevated levels of thrombin. Thrombin accumulation in neurofibrillary tangles of the brain may contribute to the aggregation of tau protein and pathophysiology of Alzheimer disease.

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 investigate the protein C pathway in intestinal barrier function.

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 from saline sodium citrate buffer, pH 6.5

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.

Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
2

Frequently Asked Questions

Which document(s) contains shelf-life or expiration date information for a given product?
If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.
How do I get lot-specific information or a Certificate of Analysis?
The lot specific COA document can be found by entering the lot number above under the "Documents" section.
Can a stock solution of Product T6884, Thrombin, be stored frozen?
A suggested stock solution is 100 units/ml. The solution should contain 0.1% BSA for stability and may be stable for about one week at 0-5°C. Since thrombin solutions adsorb to glass, it is recommended to aliquot the solutions in plastic tubes and store at -20°C or below.
How do I find price and availability?
There are several ways to find pricing and availability for our products.Once you log onto our website, you will find the price and availability displayed on the product detail page.You can contact any of our Customer Sales and Service offices to receive a quote. USA customers: 1-800-325-3010 orview local office numbers.
What is the Department of Transportation shipping information for this product?
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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