Streptavidin Agarose Resin

Streptavidin Agarose Resin is a high affinity biotin-binding chromatography resin with streptavidin covalently bound to 6% crosslinked agarose beads and a biotin binding capacity of >300 nmol/ml of gel. Immobilized Streptavidin resin is suitable for gravity flow columns, spin columns, and FPLC methods. Immobilized Streptavidin can be used for affinity chromatography purifications by separating biotinylated proteins from non-biotinylated proteins and for affinity purification of antigens when used with biotinylated antibodies.

• Superior coupling chemistry: The methods used to prepare this resin are superior to all other immobilization technologies, providing higher binding capacity, lower nonspecific binding, and less leaching.
• Superior performance: Higher binding capacity than Streptavidin agarose from other vendors (highest we know of on the market).

Streptavidin is a biotin-binding protein found in the culture broth of the bacterium Streptomyces avidinii. Streptavidin can bind to four moles of biotin per mole of protein and it shows extremely high affinity, approximately 10,000-15,000 Da. Streptavidin lacks the carbohydrate side chains present on avidin and has an isoelectric point of 6.5 to avidin's 10 far closer to that at which most useful biological interactions occur. As a result, Streptavidin frequently exhibits much lower non-specific binding than avidin does. It has an acidic pI of 5.5 and a mass of 75 kDa.

Common Streptavidin Applications:

• 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

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