Characterization of a scfv to non-muscle myosin-II

CHED 792

Sarah A. Guigui, sarah.guigui@gmail.com1, Reniqua House2, Natalya Dulyaninova2, and Anne Bresnick2. (1) Department of Chemistry and Biochemistry, Stern College for Women, Yeshiva University, 245 Lexington Avenue, New York, NY 10016, (2) Biochemistry Department, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461
Recombinant antibodies are useful tools for probing protein structure and function both in vitro and in vivo. The most prevalent recombinant antibody subunit is the scFv, or single chain variable fragment. While the scFv comprises only the variable portion of the antibody, it retains the specificity of the intact antibody molecule. In a screen against Golgi-associated proteins, a previous study identified a recombinant antibody to nonmuscle myosin-II, termed scFv SF9. To begin mapping the epitope recognized by scFv SF9 on myosin-II and to examine the isoform specificity of the scFv, we performed immunoblot analysis on several myosin-II constructs. Preliminary studies suggest that scFv SF9 binds to the rod domain of myosin-IIA and myosin-IIB. Attempts to bacterially express and purify the scFv SF9 were unsuccessful due to poor expression levels in E. coli. Future efforts will be directed at testing alternative expression systems.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008