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Safety Information

T5772

Sigma-Aldrich

Thrombin from rat plasma

lyophilized powder, ≥1,000 units/mg protein (biuret)

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About This Item

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

biological source

rat plasma

Quality Level

form

lyophilized powder

specific activity

≥1,000 units/mg protein (biuret)

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... F2(29251)
rat ... F2(29251)

General description

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

Application

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 activation of equine platelet-rich plasma.
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

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, Lot K.

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 0.1 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.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

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

Regulatory Information

动植物源性产品

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Xiaojun Chen et al.
Cell death discovery, 8(1), 189-189 (2022-04-12)
Spinal cord injury (SCI) will result in the significant elevation of thrombin production at lesion site via either breakage of blood-spinal cord barrier or upregulated expression within nerve cells. Thrombin-induced activation of the protease activated receptors (PARs) evokes various pathological
Jamie A Textor et al.
Veterinary surgery : VS, 41(7), 784-794 (2012-06-30)
To investigate and compare clinically relevant Platelet-rich plasma (PRP) activation methods. Experimental. PRP was prepared from 6 equine subjects. Activation of the PRP was performed by 4 methods (autologous thrombin, bovine thrombin, calcium chloride (CaCl(2) ), or freeze-thaw). The resultant
Ting Yang et al.
Journal of neuroinflammation, 19(1), 120-120 (2022-05-28)
The danger-associated molecular patterns (DAMPs) are critical contributors to the progressive neuropathology and thereafter affect the functional outcomes following spinal cord injury (SCI). Up to now, the regulatory mechanisms on their inducible production from the living cells remain elusive, aside
Pancras C Wong et al.
Hospital practice (1995), 41(1), 19-25 (2013-03-08)
The effect of the oral direct activated factor X (factor Xa) inhibitor apixaban on tissue factor-induced thrombin generation in human plasma was investigated in vitro using the calibrated automated thrombogram (CAT) method and compared with the oral direct factor Xa
Dabigatran: a nephrological way out.
Patricio A Pazmiño
The American journal of medicine, 126(4), e21-e21 (2013-03-20)

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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