Streptavidin-ZAP [IT-27, KIT-27]

Streptavidin-ZAP converts biotinylated materials into targeted toxins. Streptavidin is a tetrameric protein (molecular weight 53 kDa in its recombinant form), with each subunit able to bind a single biotin molecule. The bond between streptavidin and biotin is rapid and essentially non-reversible, unaffected by most extremes of pH, organic solvents, and denaturing reagents. It is the strongest known noncovalent biological interaction (Ka = 10¹⁵ M^-1) between protein and ligand. The streptavidin used to make Streptavidin-ZAP contains no carbohydrate group and has a neutral isoelectric point, which therefore reduces the nonspecific binding as compared to avidin. A variety of molecules, including lectins, proteins, and antibodies, can be biotinylated and reacted with streptavidin-labeled probes or other detection reagents for use in biological assays.

Streptavidin-ZAP is a chemical conjugate of streptavidin and the ribosome-inactivating protein, saporin. It converts biotinylated materials into targeted toxins.

Streptavidin-ZAP is available individually (Cat. #IT-27) and in multiple kit variations.