School of Biotechnology

  Staphylococcal protein A
Research groups
Human protein atlas
Mycoplasma mycoides
Antibody proteomics
Alkali stabilization
Tree genomics
Single cell analysis
Biosensor (DNA)
Surface display
Protein folding
In vivo stabilization
Solid phase methods
Protein G
Protein A
Affinity tags


The gene for the staphylococcal protein A was cloned and characterized (1, 2, 3, 4). This IgG-binding receptor was found to have evolved through multiple gene duplications (2). Several recombinant versions of the receptor (5) were developed in collaboration with Pharmacia Biotech (Uppsala, Sweden), now GE Health Care. Recombinant protein A (see figures) is now frequently used for affinity purification of monoclonal and polyclonal antibodies.
Key (own) publications:
Lofdahl, Guss, Uhlen, Philipson & Lindberg (1983) Gene for staphylococcal protein A. Proc Natl Acad Sci U S A 80, 697-701.
Uhlen, M., B. Guss, B. Nilsson, S. Gatenbeck, L. Philipson, and M. Lindberg (1984) Complete sequence of the staphylococcal gene encoding protein A. A gene evolved through multiple duplications. J Biol Chem 259, 1695-1702.
Abrahmsen, Moks, Nilsson, Hellman & Uhlen (1985) Analysis of signals for secretion in the staphylococcal protein A gene. Embo J 4, 3901-3906.
Moks, T., L. Abrahmsen, B. Nilsson, U. Hellman, J. Sjoquist, and M. Uhlen (1986) Staphylococcal protein A consists of five IgG-binding domains. Eur J Biochem 156, 637-643.
Nilsson, B., T. Moks, B. Jansson, L. Abrahmsen, A. Elmblad, E. Holmgren, C. Henrichson, T.A. Jones, and M. Uhlen (1987) A synthetic IgG-binding domain based on staphylococcal protein A. Protein Eng 1, 107-113.
Last updated: 2010-12-22