Bacterial Expression and Purification of C1C2 Domain of Human Factor VIII

Expression of Biologically Active Recombinant B-Domain-Deleted Human Factor VIII in Mammalian Cells

expression of biologically active recombinant b-domain-deleted human factor viii in mammalian cells

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Human coagulation factor VIII domain-specific recombinant polypeptide expression

BACKGROUND Hemophilia A is caused by heterogeneous mutations in F8. Coagulation factor VIII (FVIII), the product of F8, is composed of multiple domains designated A1-A2-B-A3-C1-C2. FVIII is known to interact with diverse proteins, and this characteristic may be important for hemostasis. However, little is known about domain-specific functions or their specific binding partners. METHODS To det...

Studies on the Purification and Characterization of Human Factor VIII

The purified factor VIII has been found to be a macromolecular glycoprotein with a major subunit of 240,000, as shown by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Carbohydrate analysis of factor VIII gave values of 1% sialic acid, 2.8% hexosamine, and 1-2% hexose (mannose, galactose, and fucose). The lipid content was found to be less than 5% of the protein content, and i...

Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin

Betatrophin is a member of the angiopoietin-like (ANGPTL) family that has been implicated in both triglyceride and glucose metabolism. The physiological functions and molecular targets of this protein remain largely unknown; hence, a purified available protein would aid study of the exact role of betatrophin in lipid or glucose metabolism. In this study, we cloned the full-length cDNA of betatr...

Cloning, Expression and Purification of Clostridium botulinum Neurotoxin Type E Binding Domain