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Key Documents

SAE0006

Sigma-Aldrich

Thrombin human

recombinant, expressed in HEK 293 cells, aqueous solution, ≥95% (SDS-PAGE)

Synonym(s):

Factor IIa

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in HEK 293 cells

product line

BioUltra

assay

≥95% (SDS-PAGE)

form

aqueous solution

specific activity

≥1500 units/mg protein

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... F2(2147)

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General description

Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Thrombin is also known as coagulation factor IIa.[1] It is a serine endopeptidase that hydrolyzes peptide and ester bonds specifically at the carboxylic side of arginine.[2] This enzyme converts fibrinogen to fibrin.[3]

Application

Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to assess in vitro hemostatic properties of French lyophilized plasma.†

Physical form

supplied as a solution in 20 mM MES, pH 6.0, 500 mM choline chloride

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Fibrinogen and fibrin structure and functions
M W Mosesson
Journal of Thrombosis and Haemostasis, 3 (2005)
Guidance on the emergent reversal of oral thrombin and factor Xa inhibitors
Scott Kaatz
American Journal of Hematology (2012)
Brian J Grindel et al.
ACS omega, 5(39), 25440-25455 (2020-10-13)
Directed evolution is a powerful tool for the selection of functional ligands from molecular libraries. Extracellular domains (ECDs) of cell surface receptors are common selection targets for therapeutic and imaging agent development. Unfortunately, these proteins are often post-translationally modified and
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
W Bode
Protein Science (1992)

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