Principal Investigator

Philip J. Fay, Ph.D. University of Rochester work Box 712 601 Elmwood Ave Rochester NY 14642 office: MC 3-8553 p 585-275-6756 f 585-473-4314


Fay Lab University of Rochester work MC 3-7544 601 Elmwood Ave Rochester NY 14642 p 585-275-6577


Human Factor VIII Structure & Function

Technician Amy Griffiths working in the Fay Lab

Factor VIII serves as a protein cofactor for the serine protease, factor IXa in the membrane-dependent conversion of factor X to factor Xa during the blood coagulation cascade reactions. Deficiency or defects in factor VIII result in hemophilia A, the most common of the severe, inherited bleeding disorders. Ongoing studies in our laboratory include physical and biochemical analyses of factor VIII structure, inter-subunit interactions, and intermolecular interactions with other components of the clotting cascade. Overall, our research program is aimed at gaining fundamental insights into the structure, activity and regulation of a protein central to hemostasis. This information will have specific implications for understanding hemophilia A and developing superior therapeutics for its treatment.