ExtrAvidin(R)-Agarose, high binding For purification of biotinylated macromolecules and complexes

ExtrAvidin(R) is a unique de-glycosylated Avidin modified form of an affinity purified egg white avidin. The ExtrAvidin is conjugated to cyanogen bromide-activated agarose beads.ExtrAvidin(R) is a tetrameric protein containing four biotin binding sites. The Avidin-Biotin high affinity interaction (Kd=10-15M) is considered one of the strongest non-covalent interactions known in nature. The use of Avidin-Biotin complex for affinity purification was described in the first half of 1970 and since then it was successfully utilized in numerous studies and biotechnological applications.1-3 This was achieved due to the ability to chemically coupe the small Biotin molecule with different binders, without disturbing its function or structure, thus allowing unique interaction with a variety of Avidin carriers including: protein or DNA molecules, Avidin protein bound to a solid surface matrix, reporter molecules, probes or carriers,. Among the known Avidin-Biotin interaction based applications are purification, enrichment, detection, amplification and other research medical and industrial processes. In addition, the ExtrAvidin(R) high specificity binding to Biotin, together with the low background staining, grant it significant advantage compared to the non-modified Avidin or Streptavidin produced by Streptomyces avidinii.