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10602400001

Roche

Thrombin

from human plasma

Synonym(s):
coagulation factor Iia, thrombin
Enzyme Commission number:

biological source

human plasma

Quality Level

form

lyophilized

specific activity

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

mol wt

Mr ~33.6 kDa

packaging

pkg of 20 U

manufacturer/tradename

Roche

optimum pH

8.2-9.0

shipped in

wet ice

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This Item
SRP6557SRP6556SAE0147
Thrombin from human plasma

Roche

10602400001

Thrombin

form

lyophilized

form

lyophilized

form

lyophilized

form

-

specific activity

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

specific activity

-

specific activity

-

specific activity

-

mol wt

Mr ~33.6 kDa

mol wt

37 kDa

mol wt

37 kDa

mol wt

-

manufacturer/tradename

Roche

manufacturer/tradename

-

manufacturer/tradename

-

manufacturer/tradename

-

optimum pH

8.2-9.0

optimum pH

-

optimum pH

-

optimum pH

-

General description

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.

Application

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.

Biochem/physiol Actions

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.

Physical form

Lyophilizate

Preparation Note

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

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

Reconstitution

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

Storage and Stability

Store at 2 to 8 °C. (Store dry!)

Other Notes

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

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Precautionary Statements

Hazard Classifications

Acute Tox. 4 Inhalation

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

does not flash

Flash Point(C)

does not flash


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Customers Also Viewed

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Thrombin: Physiology and Disease (2010)
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
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)
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)

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