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T6634

Sigma-Aldrich

Thrombin from bovine plasma

lyophilized powder, 600-2,000 NIH units/mg protein (biuret)

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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:
MFCD00166053
NACRES:
NA.54

form

lyophilized powder

Quality Level

300

specific activity

600-2,000 NIH units/mg protein (biuret)

mol wt

heavy chain ~33 kDa
light chain ~5 kDa

UniProt accession no.

P00735

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

cow ... F2(280685)

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This Item
T7009T4648T7513
Sigma-Aldrich

Sigma-Aldrich

T6634

Thrombin from bovine plasma

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

Sigma-Aldrich

T7009

Thrombin from human plasma

Thrombin from bovine plasma lyophilized powder, 40-300 NIH units/mg protein (biuret)

Sigma-Aldrich

T4648

Thrombin from bovine plasma

Sigma-Aldrich

Sigma-Aldrich

T7513

Thrombin from bovine plasma

specific activity

600-2,000 NIH units/mg protein (biuret)

specific activity

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

specific activity

40-300 NIH units/mg protein (biuret)

specific activity

≥2,000 NIH units/mg protein (E1%/280 = 19.5)

mol wt

heavy chain ~33 kDa, light chain ~5 kDa

mol wt

37.4 kDa

mol wt

heavy chain ~33 kDa, light chain ~5 kDa

mol wt

heavy chain ~33 kDa, light chain ~5 kDa

UniProt accession no.

P00735

UniProt accession no.

P00734

UniProt accession no.

P00735

UniProt accession no.

P00735

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

Thrombin is a sodium-activated type II enzyme. It contains two anion binding exosites, ABE-I and ABE-II. The predominant form of thrombin in vivo is the zymogen prothrombin (factor II), which is produced in the liver. Bovine a-thrombin consists of a light chain (A chain) and a heavy chain (B chain). These two chains are joined by one disulfide bond. The B chain of a-thrombin includes a carbohydrate portion.

Application

Thrombin from bovine plasma has been used to study its effect on the perinatal rat subventricular zone cells and oligodendrocyte precursor cell proliferation, differentiation, and migration in culture. It has also been used in fibrin degradation assay to measure nattokinase activity.
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 assess global haemostasis and point of care testing.

Biochem/physiol Actions

Thrombin is a proteolytic enzyme critical in the blood clotting process and activates clotting factors V, VIII, XI, and XII. Thrombin promotes platelet aggregation. Therefore, thrombin is the final coagulation protease in hemostasis, promoting both procoagulant and anticoagulant effects. It is used to treat bleeding from capillaries and small venules.
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

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.

inhibitor

Product No.
Description
Pricing

substrate

Product No.
Description
Pricing

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Thrombin, Bovine, High Activity

Thrombin as an Agent
xPharm: The Comprehensive Pharmacology Reference null
Congenital and Acquired Hypercoagulable Syndromes
The Vein Book, 339-346 (2007)
Thrombin as a Target
xPharm: The Comprehensive Pharmacology Reference null
Fergal J Duffy et al.
Journal of chemical information and modeling, 55(3), 600-613 (2015-02-11)
Protein-protein and protein-peptide interactions are responsible for the vast majority of biological functions in vivo, but targeting these interactions with small molecules has historically been difficult. What is required are efficient combined computational and experimental screening methods to choose among
Akiomi Takano et al.
Investigative ophthalmology & visual science, 47(5), 2075-2079 (2006-04-28)
To investigate the effects of intravitreal injection of nattokinase (subtilisin NAT), a serine protease that is produced by Bacillus subtilis (natto), for induction of posterior vitreous detachment (PVD). Different doses of nattokinase (1, 0.1, or 0.01 fibrin-degradation units [FU]) or
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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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