Saltar al contenido
Merck

T4393

Sigma-Aldrich

Trombina from human plasma

lyophilized powder, 1500-3500 NIH units/mg protein (E1%/280, 18.3), suitable for cell culture

Sinónimos:

Factor IIa

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.75

biological source

human plasma

Quality Level

sterility

sterile

form

lyophilized powder

specific activity

1500-3500 NIH units/mg protein (E1%/280, 18.3)

technique(s)

cell culture | mammalian: suitable

impurities

HIV, hepatitis B and hepatitis C, tested negative

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... F2(2147)

¿Está buscando productos similares? Visita Guía de comparación de productos

General description

Thrombin is produced from the proteolytic cleavage of inactive prothrombin in the liver. The prothrombin gene is mapped to human chromosome 11p11.2. It comprises of A and B catalytic domain, recognition domain and insertion loops. The active site residues comprise the catalytic tetrad, (histidine 57, aspartate 102, serine 195 and serine 214).

Application

Thrombin from human plasma has been used:
  • as a medium supplement for the pre-treatment of endothelial cell culture prior to confocal microscopy and enzyme linked immunosorbent assay (ELISA)
  • in the gelatinization of mesenchymal stem cells (MSCs) for preparing fibrin–MSC construct
  • for screening serine protease inhibitor, OGTI from frog skin secretion

Biochem/physiol Actions

The main function of thrombin is the cleavage of fibrinogen to fibrin, to assist stable clot formation. High levels of thrombin elicit neurotoxicity in dopaminergic neurons and contributes to the progression of Parkinson′s disease. A wide range of mutations in the prothrombin gene contributes to its deficiency resulting in coagulation disorders like dysprothrombinemia and hypoprothrombinemia. Altered thrombin levels modulates the coagulation pathway in multiple sclerosis. Patients with coronary artery disease (CAD) show elevated levels of thrombin. Thrombin accumulation in neurofibrillary tangles in the brain may contribute to the aggregation of τ protein and pathophysiology of Alzheimer disease.
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

Reconstitution

When reconstituted with 1 mL water, vial contains stated activity in 0.15 M sodium chloride and 0.05 M sodium citrate, 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.

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.

Substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

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»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

Endothelial cell processing and alternatively spliced transcripts of factor VIII: potential implications for coagulation cascades and pulmonary hypertension
Shovlin CL, et al.
PLoS ONE, 5(2), e9154-e9154 (2010)
Thrombin generation correlates with disease duration in multiple sclerosis (MS): Novel insights into the MS-associated prothrombotic state
Parsons MEM, et al.
Multiple Sclerosis Journal, 3(4) (2017)
Richard C Rogers et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 318(6), R1068-R1077 (2020-04-23)
Severe trauma can produce a postinjury "metabolic self-destruction" characterized by catabolic metabolism and hyperglycemia. The severity of the hyperglycemia is highly correlated with posttrauma morbidity and mortality. Although no mechanism has been posited to connect severe trauma with a loss
A small trypsin inhibitor from the frog of Odorrana grahami
Li J, et al.
Biochimie, 90(9), 1356-1361 (2008)
Chia-Chun Chen et al.
Journal of orthopaedic research : official publication of the Orthopaedic Research Society, 30(3), 393-400 (2012-01-24)
Extracellular matrix (ECM) is thought to participate significantly in guiding the differentiation process of mesenchymal stem cells (MSCs). In this study, we hypothesized that cartilage fragments from osteoarthritic knee could promote chondrogenesis of MSCs. Nonworn parts of cartilage tissues were

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.

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.

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico