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605190-M

Sigma-Aldrich

Thrombin, Human Plasma

Sinónimos:

Thrombin, Human Plasma

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About This Item

Número de CAS:
Código UNSPSC:
12352202
NACRES:
NA.51

origen biológico

human plasma

Nivel de calidad

formulario

lyophilized

actividad específica

≥1000 NIH units/mg protein

fabricante / nombre comercial

Calbiochem®

condiciones de almacenamiento

OK to freeze

solubilidad

water: 1 mg/mL
aqueous buffer: soluble

temp. de almacenamiento

−20°C

Descripción general

Thrombin, a sodium-activated type II enzyme, comprises two anion binding exosites, ABE-I and ABE-II. This serine protease enzyme is synthesized from zymogen prothrombin (factor II) in the liver.

Aplicación

Thrombin, Human Plasma has been used:
  • as a component of endothelial growth medium (EGM) media for the transplantation and reisolation of Kaposi′s sarcoma-associated herpesvirus-human endothelial cell line (KSHV-HuARLT) cells from mice
  • for the fabrication of fibrin gels
  • as a component of EGM media for viral copy number analysis of KSHV-HuARLT cells and matrigel implant

Acciones bioquímicas o fisiológicas

Thrombin cleaves and converts fibrinogen into fibrin. It then activates factors V, VIII, XI, and XIII. Thrombin stimulates platelet activation and stabilizes the fibrin polymers. It elicits a vital role in the last stages of the blood coagulation cascade.

Advertencia

Toxicity: Harmful (C)

Definición de unidad

One unit is determined by comparison with a standard curve prepared using the Bureau of Biologics standard thrombin.

Forma física

Lyophilized from 200 mM NaCl, 50 mM citrate buffer, 0.1% PEG-8000, pH 6.5. Contains BSA as a stabilizer.

Nota de preparación

Prepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitución

Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 2 months at -70°C.

Nota de análisis

Complete activation from homogeneous prothrombin by SDS-PAGE

Información legal

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Cláusula de descargo de responsabilidad

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.

Pictogramas

Health hazardExclamation mark

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

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

Órganos de actuación

Respiratory system

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°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

Segall JA and Liem TK
Congenital and Acquired Hypercoagulable Syndromes, 339-346 (2007)
Kitchens CS, et al
Consultative Hemostasis and Thrombosis (2013)
Diana L Diesen et al.
Vascular, 16 Suppl 1, S29-S36 (2008-03-01)
Thrombin is a common hemostatic drug used in surgical practice for over 100 years because of its simplicity and efficacy. Thrombin converts fibrinogen to fibrin, activates platelets, and induces vascular contraction. It is available in multiple forms, including human thrombin
Isis S R Carter et al.
Thrombosis, 2010, 416167-416167 (2010-01-01)
Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region
Dillon K Jarrell et al.
PloS one, 16(5), e0239242-e0239242 (2021-05-20)
Fibrin has been used clinically for wound coverings, surgical glues, and cell delivery because of its affordability, cytocompatibility, and ability to modulate angiogenesis and inflammation. However, its rapid degradation rate has limited its usefulness as a scaffold for 3D cell

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