Streptavidin−agarose from Streptomyces avidinii has been used:

• to pull down biotinylated cell surface proteins during the quantification of plasma membrane transforming growth factor β (TGFβ) receptor II (TβRII) and Tβ
• RII internalization
• in biotinylated miRNA pull-down assay; as secondary antibodies in immunoprecipitation

Streptavidin-agarose is used in protein chromatography, affinity chromatography, and recombinant protein expression and analysis. Streptavidin-agarose has been used to study the oriented immobilization of the tobacco etch virus protease for the cleavage of fusion proteins. Streptavidin-agarose has also been used to develop a method for screening triplex DNA binders from natural plant extracts.

Used for the purification of biotin containing proteins or DNA binding proteins

Streptavidin is a homotetrameric protein, isolated from Streptomyces avidinii, which, like avidin, has a high affinity for biotin. Streptavidin is slightly anionic (pI ~ 5-6) and non-glycosylated. These properties contribute to its relatively low non-specific binding compared to egg white avidin. Streptavidin is also more resistant than avidin to dissociation into subunits by guanidinium chloride. Streptavidin-agarose can be used to immobilize or isolate various biotinylated macromolecules and complexes (proteins, antibodies, lectins, nucleic acids, receptors, and ligands). The inherent high-affinity streptavidin-biotin interaction requires harsh conditions to release biotinylated macromolecules. This feature makes streptavidin-agarose useful in a variety of affinity purification applications.

Suspension in 0.01 M sodium phosphate, pH 7.2, containing 0.05 M NaCl and 0.02% sodium azide