Streptavidin is a tetrameric protein containing four biotin-binding sites similar to avidin. The native protein isolated from culture filtrates of Streptomyces avidinii is carbohydrate-free, has an acidic pI of 5.5 and a mass of 75 kDa. Streptavidin generally has less nonspecific binding than avidin (from chicken egg white) because of the absence of carbohydrates.

Our Streptavidin Resins (i.e., Immobilized Streptavidin Products) use a recombinant form of streptavidin with a mass of 53 kDa and a near-neutral pI. These resins are prepared by covalently coupling streptavidin to the porous agarose or UltraLink Biosupport using efficient and stable chemistries, resulting in Streptavidin Agarose and UltraLink Resins that are leach-resistant and stable at pH 2-11. 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.

Highlights:

• Proven coupling chemistries – The methods used to prepare these resins are superior to typical cyanogen bromide (CNBr) immobilization, providing high functionality, low nonspecific binding and excellent leach-resistance.
• Versatile resins – Agarose (polysaccharide-based) and UltraLink Biosupport (acrylamide-based) resins provide two different options for particular experimental conditions and are compatible with gravity-flow, spin and FPLC methods.
• Available in multiple formats – Choose from two resin types, regular or high capacity preparations, and small or large-scale package sizes (bulk sizes are also available).
• Superior performance – High Capacity Resin has 2-3 times higher binding capacity than alternative supplier products, allowing use of small amounts of resin for experiments (see streptavidin data).