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Engineered streptavidin as a versatile tool for
protein interaction studies
would like to introduce and illustrate various possible
applications of reversible binding between Strep-Tactin® and biotinylated
molecules, such as proximity-dependent biotin identification
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
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.