Streptavidin (Sepharose® Bead Conjugate) is useful for the precipitation of biotinylated proteins (1,2). Recombinant streptavidin is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads.
Background
Streptavidin is a 53,000 dalton tetrameric protein purified from the bacterium Streptomyces avidinii. Each subunit binds to biotin with extremely high affinity. Because of its strong non-covalent interaction with biotin, streptavidin can be used to isolate biotinylated proteins.
References
[1] Updyke, T.V. and Nicolson, G.L. (1984) J Immunol Methods 73, 83-95.
[2] Buckie, J.W. and Cook, G.M. (1986) Anal Biochem 156, 463-72.
[3] Chaiet, L. and Wolf, F.J. (1964) Arch Biochem Biophys 106, 1-5.
[4] Reznik, G.O. et al. (1998) Proc Natl Acad Sci U S A 95, 13525-30.
