In this study, we established a purification scheme to purify recombinant laforin and analyzed laforin to determine whether the monomer or dimer species is more physiologically relevant. Our ultimate goal is to crystallize laforin to determine its three-dimensional structure and use these insights to understand the enzyme. Human laforin is difficult to purify due to its tendency to be sequestered into inclusion bodies when expressed in E. coli. Therefore, we cloned the gene for laforin from the Gallus gallus (red rooster) genome into a bacterial expression vector and purified laforin from E. coli using a two-step purification procedure. We subjected monomeric Gallus gallus laforin to gel electrophoresis, mass spectrometry, dynamic light scattering, phosphatase and starch-binding assays.