Streptavidin−Maleimide from Streptomyces avidinii

Streptavidin conjugated compounds may be used in avidin/strepavidin:biotin-based detection systems.

Streptavidin is a protein produced by the bacterium Streptomyces avidinii. It has four binding sites for biotin, as does avidin. Both have been used extensively as probes in immunochemical systems, conjugated to antibodies, enzymes or fluorochromes. However, avidin is highly basic (pI ~ 10.5), compared to streptavidin (pI ~ 5-6). Avidin has a slightly higher binding capacity for biotin than streptavidin does, but it has glycosylated side chains which give higher backgrounds in blotting techniques than does streptavidin, which is not a glycoprotein. Streptavidin is more resistant than avidin to dissociation into subunits by guanidinium chloride.

Maleimide Activated Streptavidin is used to prepare streptavidin-protein conjugates with proteins, peptides and other molecules that contain a free sulfhydryl (-SH) group. Activated streptavidin presents an available maleimide group that reacts with sulfhydryl-containing molecules.

Lyophilized powder containing sodium citrate.

Streptavidin, from Streptomyces avidinii, activated with maleimidocaproic acid N-hydroxysuccinimide ester.

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