Open Access Research article

Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli

M Kathryn Brewer, Satrio Husodo, Vikas V Dukhande, Mary Beth Johnson and Matthew S Gentry*

Author Affiliations

Department of Molecular and Cellular Biochemistry and Center for Structural Biology, College of Medicine, University of Kentucky, 741 S. Limestone, Lexington, Kentucky 40536-0509, USA

For all author emails, please log on.

BMC Biochemistry 2014, 15:8  doi:10.1186/1471-2091-15-8

Published: 2 April 2014

Additional files

Additional file 1: Figure S1:

Multimerization of Xt-laforin. Xt-laforin was purified by IMAC and passed over a HiLoad 16/60 Superdex 200 size exclusion column. The chromatogram shows a prominent peak corresponding to a multimeric species and unresolved peaks corresponding to the Xt-laforin dimer and monomer (72 kDa and 36 kDa, respectively).

Format: PDF Size: 290KB Download file

This file can be viewed with: Adobe Acrobat Reader

Open Data