Abstract
Protein A from Staphylococcus aureus has become an important tool in immunology and molecular biology due to its specific binding to the constant region of immunoglobulins (Igs) from most mammalian species 1. Many qualitative and quantitative techniques have been developed which take advantage of this ‘pseudo-immune’ reaction 2. In addition, solid state protein A has recently been introduced in medical therapy to decrease the amount of circulating immune complexes in sera 3. In this article Mathias Uhlén, Martin Lindberg and Lennart Philipson describe the structure of the protein A molecule and its gene. They also discuss the possibilities for fusing the protein A gene to other genes.
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