Pierce™ Streptavidin Plus UltraLink™ Resin, 2 mL - FAQs

UltraLink Immobilized Streptavidin Plus Support should be used when you are planning to perform anything other than gravity filtration with a column. Streptavidin Plus UltraLink Resin is often preferred for immunoprecipitation because the white appearance of the support allows the pellet to be visualized more easily than the translucent pellet of agarose supports.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

The biotin-binding capacity is >3 mg biotinylated BSA/ml of resin, or >120 nMoles biotin/mL of resin which is equilvalent to approximately 30 µg of biotin or 30 units of biotin/ml.

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The binding affinity of streptavidin is similar to that of avidin, which is Ka = 10^15/M.

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UltraLink Biosupport Medium is stronger than agarose, being capable of withstanding 100 p.s.i. The support starts with an azlactone ring that opens upon immobilization of a ligand to form a five-molecule spacer arm.

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Steric hindrance can interfere with the binding. As with avidin, the double ring structure of biotin must fit 9 angstroms into the streptavidin molecule for binding to occur. Competitive inhibition by endogenous biotin may also interfere with binding of your biotinylated ligand.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Yes. Biotinylate your capture ligand and incubate it with the support. The biotin will bind the ligand to the support. The support can now be used to pull down molecules with an affinity for the ligand, and these molecules can be eluted using standard elution buffers without fear of contamination from the biotinylated ligand.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

The conditions necessary for elution are very harsh. To elute the biotin, the streptavidin must be irreversibly denatured via one of two common methods: boiling in SDS-PAGE sample buffer or incubation with 8 M guanidine chloride, pH 1.5. When working with a small biotinylated ligand, sometimes even the latter elution method is not strong enough to recover the entire sample. With either of these elution methods, the support cannot be reused due to the destruction of the streptavidin.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.