Title

Using Antibodies to Study Where Proteins Bind Together: A Preliminary Analysis of BEX-1 and EPRS Binding Domains

Abstract

My lab studies BEX-1, a little-understood protein that may be related to heart disease. Recently, we learned that BEX-1 might bind with another protein called EPRS. This protein plays an important role in both constructing protein building-blocks and in inhibiting protein synthesis. This binding interaction suggests that BEX-1 and EPRS affect the activity of each other in the cell. By learning where these two proteins attach, we can begin to ascertain how they would affect each other. To do this, I grew cells that expressed certain parts of BEX-1 and EPRS. I then used antibodies to isolate proteins and detect any other proteins bound to it. This technique is called a co-immunoprecipitation. My work helped verify protein sizes, overcome cell expression problems, and bring the lab several steps closer to characterizing how BEX-1 and EPRS interact.

Faculty Sponsor

Ginger Withers

Tracks

poster

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Location

Cordiner Hall

Presentation Type

Poster

Research Funding Source or OCS Program

National Science Foundation, Ohio State University RNA Center for Biology

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Using Antibodies to Study Where Proteins Bind Together: A Preliminary Analysis of BEX-1 and EPRS Binding Domains

Cordiner Hall

My lab studies BEX-1, a little-understood protein that may be related to heart disease. Recently, we learned that BEX-1 might bind with another protein called EPRS. This protein plays an important role in both constructing protein building-blocks and in inhibiting protein synthesis. This binding interaction suggests that BEX-1 and EPRS affect the activity of each other in the cell. By learning where these two proteins attach, we can begin to ascertain how they would affect each other. To do this, I grew cells that expressed certain parts of BEX-1 and EPRS. I then used antibodies to isolate proteins and detect any other proteins bound to it. This technique is called a co-immunoprecipitation. My work helped verify protein sizes, overcome cell expression problems, and bring the lab several steps closer to characterizing how BEX-1 and EPRS interact.

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