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Merck

T6634

Sigma-Aldrich

Trombina from bovine plasma

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

Sinónimos:

Factor IIa

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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

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.
Serín proteasa que hidroliza selectivamente los enlaces Arg-Gly en el fibrinógeno para formar fibrina y fibrinopéptidos A y 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

En el procedimiento de análisis NIH se utilizan 0,2 ml de plasma diluido (1:1 con disolución salina) como sustrato y 0,1 ml de muestra de trombina (estabilizada en una disolución de albúmina tamponada al 1 %), basado en una modificación del método de Biggs. Para determinar las concentraciones de trombina sólo se utilizan los tiempos de coagulación comprendidos entre 15 y 25 segundos.
La actividad se expresa en unidades NIH obtenidas por comparación directa con el patrón de referencia de la trombina NIH, lote K.

Other Notes

View more information on thrombin at www.sigma-aldrich.com/enzymeexplorer.

Substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Thrombin as a Target
xPharm: The Comprehensive Pharmacology Reference null
Thrombin as an Agent
xPharm: The Comprehensive Pharmacology Reference null
Congenital and Acquired Hypercoagulable Syndromes
The Vein Book, 339-346 (2007)
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
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

Artículos

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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