Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli
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
BMC Biochemistry 2014, 15:8 doi:10.1186/1471-2091-15-8Published: 2 April 2014
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).
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