Purification of a C1-C2 Domain Fusion Protein From Blood Coagulation Factor VIII.
Research Mentor(s)
Spiegel, P. Clint
Description
FVIII is an important clotting protein in humans and individuals without Factor VIII develop Hemophilia A. Previous research shows treatment for Hemophilia A is obstructed due to formation of inhibitory antibodies, allowing my work to determine the specific interactions and possible conformational domain shifts caused by this binding. FVIII C-domain have also been shown to be essential in binding to activated platelets during the formation of a clot therefore yielding way for research into the way FVIII interacts with phospholipids on these activated surfaces. This poster highlights the methods used to obtained purified C1-C2 domain fusion protein for these binding studies.
Document Type
Event
Start Date
16-5-2018 12:00 AM
End Date
16-5-2018 12:00 AM
Department
Chemistry
Genre/Form
student projects, posters
Subjects – Topical (LCSH)
Hemophilia; Blood coagulation disorders; Blood coagulation factor VIII antibodies
Type
Image
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this document for commercial purposes, or for financial gain, shall not be allowed without the author’s written permission.
Language
English
Format
application/pdf
Purification of a C1-C2 Domain Fusion Protein From Blood Coagulation Factor VIII.
FVIII is an important clotting protein in humans and individuals without Factor VIII develop Hemophilia A. Previous research shows treatment for Hemophilia A is obstructed due to formation of inhibitory antibodies, allowing my work to determine the specific interactions and possible conformational domain shifts caused by this binding. FVIII C-domain have also been shown to be essential in binding to activated platelets during the formation of a clot therefore yielding way for research into the way FVIII interacts with phospholipids on these activated surfaces. This poster highlights the methods used to obtained purified C1-C2 domain fusion protein for these binding studies.