Streptavidin is a 55kDa tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin (sc-204706). Streptavidin is wildly used in molecular biology through its unique high affinity for the biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~1015 M. The strong affinity of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution. The complexes are also extremely stable over a wide range of temperature and pH. The Streptavidin preparation contains an N- and C-terminal shortened variant (core streptavidin) with improved properties concerning homogeneity, solubility, resistance towards proteolytic degradation and accessibility of the biotin binding pocket as compared to native streptavidin. Streptavidin has a molecular weight of 55kDa.
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