Sanjit, We routinely use Protein G coupled resins for purification of monoclonals produced in the facility. On a structural level, antibodies typically recognize 5 or more residues in a protein unless the immunogen, such as a single amino acid in your case, is a hapten conjugated to a carrier molecule.
Could you be more specific regarding your rationale and why conventional methods (e.g. Protein A or G) are not appropriate for purifying a monoclonal antibody? Best, David -- David L. Blum, Ph.D. Bioexpression and Fermentation Facility Department of Biochemistry and Molecular Biology University of Georgia 120 Green Street room A414A Athens, GA 30602 http://bff.uga.edu/ (706) 542-1035 (Office) On Tue, May 13, 2014 at 7:32 AM, Sanjit Roy <sanjitkr...@gmail.com> wrote: > Dear All > I am planning to purify monoclonal antibody. In this > concern I found Pseudospecific ligands such as histidine, > tryptophan,phenylalanine etc. can be used to purify a wide range of > bio-molecules and especially immunoglobulin. I wish to know the structural > mode of binding of Histidine (as affinity ligand) with Immunoglobulin. > Sanjit Kumar >
