SAE0006
Thrombin human
recombinant, expressed in HEK 293 cells, aqueous solution, ≥95% (SDS-PAGE)
Synonym(s):
Factor IIa
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. It is a serine endopeptidase that hydrolyzes peptide and ester bonds specifically at the carboxylic side of arginine. This enzyme converts fibrinogen to fibrin.
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 Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Guidance on the emergent reversal of oral thrombin and factor Xa inhibitors
Scott Kaatz
American Journal of Hematology (2012)
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)
Fibrinogen and fibrin structure and functions
M W Mosesson
Journal of Thrombosis and Haemostasis, 3 (2005)
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
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