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Publication : Cloning and recombinant expression of mouse coagulation factor X.

First Author  Heidtmann HH Year  1998
Journal  Thromb Res Volume  92
Issue  1 Pages  33-41
PubMed ID  9783672 Mgi Jnum  J:50651
Mgi Id  MGI:1307057 Doi  10.1016/s0049-3848(98)00110-8
Citation  Heidtmann HH, et al. (1998) Cloning and recombinant expression of mouse coagulation factor X. Thromb Res 92(1):33-41
abstractText  Engineering of recombinant coagulation factor X variants, which can be activated by tumor-associated proteinases may lead to the development of new therapeutic molecules. However, the evaluation of such variants requires an appropriate animal model. Therefore, we isolated the complete coding sequence of mouse coagulation factor X from mouse liver cDNA by polymerase chain reaction. The deduced amino acid sequence codes for a prepro protein of 481 amino acids homologous to factor X sequences from various species. Recombinant mouse factor X was expressed in human embryonic kidney cells and secreted into cell culture supernatant as zymogen, which could be converted to catalytically active factor Xa by Russell's viper venom. Purified recombinant mouse factor X restored coagulation in human factor X deficient plasma, demonstrating that mouse factor X is able to functionally interact with the human blood coagulation system. Recombinant mouse factor X opens the possibility to analyze therapeutically useful variants in the mouse system.
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