Streptavidin, a tetrameric protein secreted by Streptomyces avidinii, binds tightly to a small growth factor biotin. It finds wide use in molecular biology through its extraordinarily strong affinity for the vitamin biotin; the dissociation constant (Kd) of the biotin-streptavidin complex is on the order of ~10-15 mol/L. The high affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. Recombinant Streptomyces streptavidin protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.