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T7009

Sigma-Aldrich

Thrombin from human plasma

lyophilized powder, ≥1,000 NIH units/mg protein (E1%/280, 18.3)

Synonym(s):

Factor IIa

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About This Item

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

form

lyophilized powder

Quality Level

specific activity

≥1,000 NIH units/mg protein (E1%/280, 18.3)

mol wt

37.4 kDa

impurities

HIV and HBsAg, source material tested negative

UniProt accession no.

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

human ... F2(2147)

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General description

The F2 gene encodes thrombin protein and is mapped to human chromosome 11p11.2.

Application

Thrombin from human plasma has been:
  • dissolved in CaCl2 and added to poly ethylene glycolated fibrinogen/cell solution for fibrin production
  • to polymerize fibrin on well plates
  • used as an endogenous agonist proteinase for proteinase-activated receptors : PAR1, PAR3 and PAR4 for stimulation of cells

Biochem/physiol Actions

Thrombin is an endolytic serine protease which stimulates vascular damage induced-leukocytes, platelets, endothelial and mesenchymal cell production. This action is mediated via G-protein-coupled receptor. It catalysis the cleavage of fibrinogen at Arg−Gly bonds to form fibrin and release fibrinopeptides A and B. The predominant form of thrombin in vivo is the zymogen prothrombin (factor II), which is produced in the liver. Prothrombin is a coagulation activation factor, high levels of which indicates cancer. Thrombin can be used to cleave fusion proteins. Cleavage of fusion proteins can be carried out at a thrombin:fusion protein ratio of 1:500.
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

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Signal transduction for proteinase-activated receptor-2-triggered prostaglandin E2 formation in human lung epithelial cells
Kawao N, et al.
Journal of Pharmacology and Experimental Therapeutics, 315(2), 576-589 (2005)
New vectors for high level expression of recombinant proteins in bacteria
Hakes DJ and Dixon JE
Analytical biochemistry, 202(2), 293-298 (1992)
B J Biemond et al.
Circulation, 96(5), 1612-1615 (1997-10-07)
In many case-control as well as epidemiological studies, increased lipoprotein(a) [Lp(a)] levels are considered to constitute an independent risk factor for premature coronary artery and cerebrovascular disease. Lp(a) resembles an LDL particle with an additional linked protein [apolipoprotein(a), apo(a)], whose
Capillary-like network formation by human amniotic fluid-derived stem cells within fibrin/poly (ethylene glycol) hydrogels
Benavides OM, et al.
Tissue Engineering: Part A, 21(7-8), 1185-1194 (2015)
Protease-activated receptor 3 is a second thrombin receptor in humans
Ishihara H, et al.
Nature, 386(6624), 502-502 (1997)

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.

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.

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.

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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