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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:
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

biological source

human plasma

Quality Level

200

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.

P00734

storage temp.

−20°C

Gene Information

human ... F2(2147)

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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.

inhibitor

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Description
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substrate

Product No.
Description
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Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

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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  1. 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.

  2. 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.

  3. 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.

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  5. 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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Thrombin generation correlates with disease duration in multiple sclerosis (MS): Novel insights into the MS-associated prothrombotic state
Parsons MEM, et al.
Multiple Sclerosis Journal, 3(4) (2017)
Howard Kim et al.
PloS one, 6(6), e21744-e21744 (2011-07-09)
Neural stem/progenitor cells (NSPCs) have great potential as a cell replacement therapy for spinal cord injury. However, poor control over transplant cell differentiation and survival remain major obstacles. In this study, we asked whether dibutyryl cyclic-AMP (dbcAMP), which was shown
Platelet subpopulations remain despite strong dual agonist stimulation and can be characterised using a novel six-colour flow cytometry protocol
Sodergren ALand Ramstrom S
Scientific reports, 8(1), 1441-1441 (2018)
Substrate stiffness combined with hepatocyte growth factor modulates endothelial cell behavior
Chang H, et al.
Biomacromolecules, 17(9), 2767-2776 (2016)
Maike Gallwitz et al.
PloS one, 7(2), e31756-e31756 (2012-03-03)
Thrombin is one of the most extensively studied of all proteases. Its central role in the coagulation cascade as well as several other areas has been thoroughly documented. Despite this, its consensus cleavage site has never been determined in detail.
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.

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