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Engineered streptavidin as a versatile tool for protein interaction studies
we would like to introduce and illustrate various possible applications of reversible binding between Strep-Tactin® and biotinylated molecules, such as proximity-dependent biotin identification (BioID).
The high affinity of streptavidin to biotin is widely used in biotechnology to isolate biotinylated molecules, but makes their elution difficult. Lower affinity of engineered streptavidin, Strep-Tactin®, allows reversible binding of biotinylated molecules making it particularly suitable for their purification.
Here we explain the BioID principle, as well as provide the links to scientific papers illustrating the versatile use of our Strep-tag® platform in BioID experiments.
We have also prepared an applicaton note highlighting the advanatges of applying Strep-Tactin® in BioID. The corresponding protocol describes the complete procedure for purification of biotinylated molecules using Strep-Tactin®.
Specific Elution and Avoidanceof Contaminations in BioID
During BioID, the biotinylated proteins are enriched from cell lysates through affinity purification, usually via matrices coated with streptavidin.
This application note explains and illustrates, why Strep-Tactin® is a preferable alternative to streptavidin for the enrichment.
View Application Note
Purification of Biotinylated Proteins with Strep-Tactin®
This step-by-step protocol provides the complete workflow for purification of biotinylated molecules starting with the sample preparation.The procedure is described for purification with both gravity flow columns and for batch purification with magentic beads. The protocol also includes the list of all necessary materials, as well as recommended buffers for washing and elution.
View Protocol