Poster Title

Novel Attempt at Expression of Properly Folded C1, C1C2, and A2 Factor VIII Protein Domains in E. coli cells

Co-Author(s)

Hali Willis

Research Mentor(s)

Clint Spiegel

Affiliated Department

Chemistry

Sort Order

31

Start Date

14-5-2015 10:00 AM

End Date

14-5-2015 2:00 PM

Document Type

Event

Abstract

Hemophilia A is a bleeding disorder treated with synthetic blood coagulation factor VIII (fVIII). In order to study fVIII we currently must use protein grown exclusively in human cell lines - a process requireing bio-safety clearance II which can be prohibitively expensive. Previous attempts to express and purify domains of fVIII in prokaryotic cells have resulted in improperly folded protein eluting in the insoluble fraction, rendering it unusable. Here we covalently bind thioredoxine to the A2, C1C2, and C1 domains of the fVIII protein and grow them in SHuffle T7 express cell line in an attempt to keep the protein properly folded and soluble.

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May 14th, 10:00 AM May 14th, 2:00 PM

Novel Attempt at Expression of Properly Folded C1, C1C2, and A2 Factor VIII Protein Domains in E. coli cells

Chemistry

Hemophilia A is a bleeding disorder treated with synthetic blood coagulation factor VIII (fVIII). In order to study fVIII we currently must use protein grown exclusively in human cell lines - a process requireing bio-safety clearance II which can be prohibitively expensive. Previous attempts to express and purify domains of fVIII in prokaryotic cells have resulted in improperly folded protein eluting in the insoluble fraction, rendering it unusable. Here we covalently bind thioredoxine to the A2, C1C2, and C1 domains of the fVIII protein and grow them in SHuffle T7 express cell line in an attempt to keep the protein properly folded and soluble.