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Key Documents

10602400001

Roche

Thrombin

from human plasma

Sinonimo/i:

coagulation factor Iia, thrombin

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About This Item

Classificazione EC (Enzyme Commission):
Codice UNSPSC:
12352204

Origine biologica

human plasma

Livello qualitativo

Forma fisica

lyophilized

Attività specifica

~120 units/mg protein (At 25 °C with Chromozym TH as the substrate.)

PM

Mr ~33.6 kDa

Confezionamento

pkg of 20 U

Produttore/marchio commerciale

Roche

pH ottimale

8.2-9.0

Condizioni di spedizione

wet ice

Descrizione generale

Thrombin is a Na+ activated allosteric serine protease. It belongs to chymotrypsin family. Thrombin is made of two polypeptide chains of 36 (A chain) and 259 (B chain) residues that are covalently attached with a disulfide bond.
Thrombin is a coagulation factor IIa. It is a serine endopeptidase that hydrolyzes peptide and ester bonds specifically at the carboxylic side of Arg. The enzyme converts fibrinogen to fibrin. The product contains EDTA and additional stabilizing agents.

Applicazioni

Thrombin has been used in the expression and purification of recombinant RELM (resistin-like moleculefamily members. It has also been used in platelet spreading on fibrinogen and immunostaining.
Thrombin is used in coagulation research, medical research, protein-structure analysis, and biochemical research. It has been used for the stimulation of the platelets.

Azioni biochim/fisiol

Thrombin plays an important role in blood coagulation. It serve as a procoagulant factor while transforming fibrinogen into an insoluble fibrin clot. Thrombin can act as anticoagulant by the activation of protein C.

Stato fisico

Lyophilizate

Nota sulla preparazione

Storage conditions (working solution): -15 to -25°C

Inhibitors: DFP, TLCK, PMSF, benzamidine, α1-antitrypsin, α2-macroglobulin, antithrombin III heparin, hirudin, and APMSF

Ricostituzione

The reconstituted solution contains 20 mM EDTA.
Important note:
Use plastic vials and pipettes because thrombin will be adsorbed to glass surfaces!

Stoccaggio e stabilità

Store at 2 to 8 °C. (Store dry!)

Altre note

For life science research only. Not for use in diagnostic procedures.

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.

Pittogrammi

Exclamation markHealth hazard

Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

Acute Tox. 4 Inhalation - STOT RE 2

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

does not flash

Punto d’infiammabilità (°C)

does not flash


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

Sigma-Aldrich

T4393

Trombina

Sigma-Aldrich

Sigma-Aldrich

1.12374

Thrombin

Trombina 400-1000 NIH units/mg protein

Sigma-Aldrich

T7572

Trombina

Trombina lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280 = 19.5)

Sigma-Aldrich

T7513

Trombina

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

Sigma-Aldrich

T6634

Trombina

Scott Kaatz et al.
American journal of hematology, 87 Suppl 1, S141-S145 (2012-04-05)
The new oral anticoagulants dabigatran, rivaroxaban and apixaban have advantages over warfarin which include no need for laboratory monitoring, less drug-drug interactions and less food-drug interactions. However, there is no established antidote for patients who are bleeding or require emergent
M W Mosesson
Journal of thrombosis and haemostasis : JTH, 3(8), 1894-1904 (2005-08-17)
Fibrinogen molecules are comprised of two sets of disulfide-bridged Aalpha-, Bbeta-, and gamma-chains. Each molecule contains two outer D domains connected to a central E domain by a coiled-coil segment. Fibrin is formed after thrombin cleavage of fibrinopeptide A (FPA)
Partially defective store operated calcium entry and Hem (ITAM) signaling in platelets of serotonin transporter deficient Mice.
Wolf K, et al.
PLoS ONE, 11(1), e0147664-e0147664 (2016)
W Bode et al.
Protein science : a publication of the Protein Society, 1(4), 426-471 (1992-04-01)
Thrombin is a multifunctional serine proteinase that plays a key role in coagulation while exhibiting several other key cellular bioregulatory functions. The X-ray crystal structure of human alpha-thrombin was determined in its complex with the specific thrombin inhibitor D-Phe-Pro-Arg chloromethylketone
Hsiao-Chuan Liu et al.
Journal of biophotonics, 14(3), e202000364-e202000364 (2020-12-15)
Embolectomy is one of the emergency procedures performed to remove emboli. Assessing the composition of human blood clots is an important diagnostic factor and could provide guidance for an appropriate treatment strategy for interventional physicians. Immunostaining has been used to

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