Streptavidin-ZAP [IT-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.

These kits convert biotinylated materials into targeted toxins and will allow you to evaluate the ability of your reagent to internalize upon binding to its receptor.