In article <mailman.721.1276024887.25217.meth...@net.bio.net>, us...@ufl.edu says... > > Hi All > I am trying to purify His-tagged protein from a halophilic (2M > NaCl)archaea which is around 30kDa. I was succesful in purifying > thro nickel column. When I run the His purified protein sample > (after dialysis in Tris buffer containing 2M NaCl, dilaysis also > helps to remove excess immidazol from the protein) on to the > gelfiltration coulumn(superdex 200), it was eluting at a molecular > weight of ~460kDa. I dont know whether the protein is getting > complexed or aggregated? But shows single band on SDS Page. > Can any one has the similar problem? Any help please? > Thanks, Siva
Is the protein you isolate biologically active? What is the size of the protein when isolated from its biological source (no GM)? _______________________________________________ Methods mailing list Methods@net.bio.net http://www.bio.net/biomail/listinfo/methods
