T6634
Thrombin from bovine plasma
lyophilized powder, 600-2,000 NIH units/mg protein (biuret)
Synonym(s):
Factor IIa
form
lyophilized powder
Quality Level
specific activity
600-2,000 NIH units/mg protein (biuret)
mol wt
heavy chain ~33 kDa
light chain ~5 kDa
UniProt accession no.
application(s)
diagnostic assay manufacturing
storage temp.
−20°C
Gene Information
cow ... F2(280685)
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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
Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.
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.
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
Activity is expressed in NIH units obtained by direct comparison to a NIH thrombin reference standard.
View more information on thrombin at www.sigma-aldrich.com/enzymeexplorer.
Signal Word
Danger
Hazard Statements
Precautionary 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
低风险生物材料
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Hongkai Xiang et al.
The Journal of international medical research, 48(9), 300060520957541-300060520957541 (2020-09-26)
To assess changes in plasma exosome levels and protein content in mice after long-term exercise. We subjected 9-month-old adult C57BL/6J mice to daily treadmill running exercise for 4 weeks prior to the isolation of blood-derived exosomes. Exosomal proteins were identified
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
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
Y Dargaud et al.
Haemophilia : the official journal of the World Federation of Hemophilia, 18 Suppl 4, 81-88 (2012-06-29)
The evaluation of the coagulation profile has used so far either clotting-based or chromogenic assays with different endpoints. Clotting-based techniques are the most used worldwide, and they certainly are useful for diagnosis of clotting factor deficiencies. However, the information provided
Congenital and Acquired Hypercoagulable Syndromes
The Vein Book, 339-346 (2007)
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.
凝血酶因子IIa是一种内切丝氨酸蛋白酶，可选择性地裂解纤维蛋白原的Arg -Gly键，形成纤维蛋白并释放纤维蛋白肽A和B。
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