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Merck

605190-M

Thrombin, Human Plasma

Sinonimo/i:

Thrombin, Human Plasma

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Informazioni su questo articolo

Numero CAS:
9002-04-4
Numero MDL:
MFCD00007020
Codice UNSPSC:
12352202
NACRES:
NA.51

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Origine biologica

human plasma

Livello qualitativo

100

Descrizione

Merck USA index - 14, 9383

Stato

lyophilized

Attività specifica

≥1000 NIH units/mg protein

Produttore/marchio commerciale

Calbiochem®

Condizioni di stoccaggio

OK to freeze

Solubilità

water: 1 mg/mL
aqueous buffer: soluble

Temperatura di conservazione

−20°C

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Questo articolo
T6884T1063T8885
Thrombin, Human Plasma

Sigma-Aldrich

605190-M

Thrombin, Human Plasma

Trombina lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280, 18.3)

Sigma-Aldrich

T6884

Trombina

Trombina lyophilized powder, ≥2800 NIH units/mg protein (E1%/280, 18.3)

Sigma-Aldrich

T1063

Trombina

Trombina lyophilized powder, Suitable for routine use in the thrombin time test

Sigma-Aldrich

T8885

Trombina

specific activity

≥1000 NIH units/mg protein

specific activity

≥2,000 NIH units/mg protein (E1%/280, 18.3)

specific activity

≥2800 NIH units/mg protein (E1%/280, 18.3)

specific activity

-

biological source

human plasma

biological source

human plasma

biological source

-

biological source

human plasma

form

lyophilized

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

solubility

water: 1 mg/mL, aqueous buffer: soluble

solubility

-

solubility

-

solubility

-

storage condition

OK to freeze

storage condition

-

storage condition

-

storage condition

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Descrizione generale

Thrombin, a sodium-activated type II enzyme, comprises two anion binding exosites, ABE-I and ABE-II.[1] This serine protease enzyme is synthesized from zymogen prothrombin (factor II) in the liver.[1][2]

Applicazioni

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[3]
  • for the fabrication of fibrin gels[4]
  • as a component of EGM media for viral copy number analysis of KSHV-HuARLT cells and matrigel implant[5]

Azioni biochim/fisiol

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.[6][7] It elicits a vital role in the last stages of the blood coagulation cascade.[1]

Stato fisico

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

Nota sulla preparazione

Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 2 months at -70°C.
Prepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Risultati analitici

Complete activation from homogeneous prothrombin by SDS-PAGE

Altre note

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

Note legali

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

Esclusione di responsabilità

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.
Toxicity: Harmful (C)

Pittogrammi

Health hazardExclamation mark
GHS08,GHS07

Avvertenze

Danger

Indicazioni di pericolo

H315,H319,H334,H335

Classi di pericolo

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

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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Kitchens CS, et al
Consultative Hemostasis and Thrombosis (2013)
Segall JA and Liem TK
Congenital and Acquired Hypercoagulable Syndromes, 339-346 (2007)
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
Madhavi A Jadhav et al.
Biochemistry, 49(13), 2918-2924 (2010-03-12)
The formation of a blood clot involves the interplay of thrombin, fibrinogen, and Factor XIII. Thrombin cleaves fibrinopeptides A and B from the N-termini of the fibrinogen Aalpha and Bbeta chains. Fibrin monomers are generated that then polymerize into a
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