Streptavidin is a tetrameric protein containing four biotin binding sites and lacks a carbohydrate, which significantly reduces the amount of non-specific binding.
Streptavidin Agarose Resin is a high affinity biotin-binding chromatography resin with streptavidin covalently bound to 6% crosslinked agarose beads with high affinity for biotin binding (>300 nmol/ml of gel). Immobilized Streptavidin resin is suitable for gravity flow columns, spin columns, and FPLC methods.
Streptavidin-agarose is used in protein chromatography, affinity chromatography, and recombinant protein expression and analysis. Streptavidin-agarose has been used to study the oriented immobilization of the tobacco etch virus protease for the cleavage of fusion proteins. Streptavidin-agarose has also been used to develop a method for screening triplex DNA binders from natural plant extracts.
The methods used to prepare this resin are superior to all other immobilization technologies, providing higher binding capacity, lower nonspecific binding, and less leaching.
Streptavidin Agarose Resins supply immobilized streptavidin biotin-binding protein in different resin formats, binding capacities and package sizes to suit nearly any immunoprecipitation or affinity purification procedure involving biotinylated molecules. The products are excellent choices for a variety of small- or large-scale affinity purification applications involving biotinylated macromolecules, including separation of biotinylated molecules from samples and immunoprecipitation of antigens using biotin-labeled antibodies.
- Purification of membrane antigens in conjunction with biotinylated monoclonal antibodies
- Cell-surface labeling with biotinylation reagents, followed by precipitation with immobilized streptavidin
- Purification of cell-surface glycoproteins using biotinylated Concanavalin A
- Recovery of single-stranded biotinylated DNA for dideoxy sequencing
Storage/Handling: Store at 4°C. Do not freeze.
1 ml, 5 ml, 10 ml