Event Title

Purification of a C1-C2 Domain Fusion Protein From Blood Coagulation Factor VIII.

Research Mentor(s)

Clint Spiegel

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

May 2018

End Date

May 2018

Location

Chemistry

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

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Purification of a C1-C2 Domain Fusion Protein From Blood Coagulation Factor VIII.

Chemistry

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.