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T6884

Sigma-Aldrich

Thrombin from human plasma

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

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Synonym(s):
Factor IIa
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

human plasma

Quality Level

form

lyophilized powder

specific activity

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

mol wt

37.4 kDa

impurities

HIV and HBsAg, source material tested negative

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... F2(2147)

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This Item
T7572T4393T8885
vibrant-m

T6884

Thrombin from human plasma

vibrant-m

T7572

Thrombin from human plasma

vibrant-m

T4393

Thrombin from human plasma

vibrant-m

T8885

Thrombin from human plasma

Gene Information

human ... F2(2147)

Gene Information

human ... F2(2147)

Gene Information

human ... F2(2147)

Gene Information

human ... F2(2147)

specific activity

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

specific activity

400-1000 NIH units/mg protein

specific activity

1500-3500 NIH units/mg protein (E1%/280, 18.3)

specific activity

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

37.4 kDa

mol wt

-

mol wt

-

mol wt

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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.
Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.

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

Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags.

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.

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.

pictograms

Exclamation markHealth hazard

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Articles

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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