High Capacity Streptavidin Agarose Resin

UBPBio High Capacity Streptavidin Agarose Resin is an affinity chromatography medium designed for easy, one-step purification of biotinylated peptides, antibodies, lectins, etc from samples. The purified recombinant streptavidin is covalently coupling to 4% highly cross-linked agarose. The coupling is optimized to give high binding capacity for biotinylated molecules. The total binding capacity of Streptavidin Resin is more than 120 nmol of D-Biotin/ml settled resin.

Streptavidin is a biotin-binding protein found in the culture broth of the bacterium Streptomyces avidinii. Streptavidin binds 4 moles of biotin per mole of protein with an extremely high affinity. Streptavidin lacks carbohydrate side chains present on avidin and has an isoelectric point of 6.5 (vs 10 for avidin) close to where most useful biological interactions occur. As a result, streptavidin frequently exhibits much lower non-specific binding than avidin does.

Additional Information

Product Name: High Capacity Streptavidin Agarose Resin
Catalog No.: P3070-5
Size: 5 ml
Bead (Geometry, size): 90 μm (45-165 μm)
Cross-Linked: Yes
Ligand: Streptavidin
Agarose %: 4% Agarose
Binding Capacity: More than 120 nmol of D-biotin per ml of column-volume
Volume %: 50% (v/v) aqueous suspended in 1X PBS containing 20% ethanol
Storage Temperature: 2-8 °C
Application: Batch, Gravity
PDF Data Sheet: Datasheet, MSDS
User's Manual: User’s G
Image(s): No
Shipping Method: Wet ice shipping

Details

UBPBio High Capacity Streptavidin Agarose Resin is an affinity chromatography medium designed for easy, one-step purification of biotinylated peptides, antibodies, lectins, etc from samples. The purified recombinant streptavidin is covalently coupling to 4% highly cross-linked agarose. The coupling is optimized to give high binding capacity for biotinylated molecules. The total binding capacity of Streptavidin Resin is more than 120 nmol of D-Biotin/ml settled resin. Streptavidin is a biotin-binding protein found in the culture broth of the bacterium Streptomyces avidinii. Streptavidin binds 4 moles of biotin per mole of protein with an extremely high affinity. Streptavidin lacks carbohydrate side chains present on avidin and has an isoelectric point of 6.5 (vs 10 for avidin) close to where most useful biological interactions occur. As a result, streptavidin frequently exhibits much lower non-specific binding than avidin does.