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

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7 product FAQs found

When should the UltraLink Immobilized Streptavidin Plus Support be used in place of streptavidin immobilized on agarose?

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.

What is the biotin-binding capacity for UltraLink Biosupport Medium?

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.

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

What is the affinity of streptavidin for biotin in the Thermo Scientific Streptavidin Plus Ultralink Resin kit?

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

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

What is UltraLink Biosupport Medium?

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.

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

What can prevent biotin from binding to the immobilized streptavidin when using the Thermo Scientific Streptavidin Plus Ultralink Resin?

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.

Can I make an affinity support using the Thermo Scientific Streptavidin Plus Ultralink Resin?

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.

After my biotinylated ligand is bound to the support when using the Thermo Scientific Streptavidin Plus Ultralink Resin, what conditions are needed to elute it from the support?

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.