Abstract
S100 proteins belong to a family of small, acidic, EF-hand Ca ( 2+) -binding proteins and have been found to exert both intracellular and extracellular functions in regulation of Ca ( 2+) homeostasis, cytoskeletal dynamics, cell cycle, motility and differentiation. As a result, they have been widely investigated for their association with diseases, such as, neurological diseases, cardiomyopathy, neoplasias and inflammatory diseases. To facilitate further studies of S100 proteins, we reported a simple and efficient method for the expression and purification of human S100A4 and S100A11 proteins in Escherichia coli. Since S100 proteins share many common physical and chemical characteristics, we expect that this approach can be extended to the production of most S100 proteins.