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Strep-tag® protein purification cycle

IBA’s unique Strep-tag® technology is a commonly used tool for the affinity purification of recombinant proteins and is based on one of the strongest non-covalent interactions in nature, which is the interaction of biotin to streptavidin. The system includes two affinity tags: Strep-tag®II and Twin-Strep-tag® (the tandem version of the Strep-tag®II). These peptide sequences exhibit intrinsic affinity towards two specifically engineered streptavidin variants — Strep-Tactin® and Strep-Tactin®XT. The system is distinguished by an easy one-step purification procedure. First, a sample containing Strep-tag® fusion proteins and non-tagged proteins is applied to the agarose beads coated with Strep-Tactin®XT. Only Strep-tag® proteins bind specifically via the tag to the biotin binding pocket of Strep-Tactin®XT. Then all non-tagged proteins are washed keeping only the specifically bound Strep-tag® fusion proteins. The specific elution of Strep-tag® proteins is achieved by using the competitor biotin in excess. After removing the bound competitor with the respective regeneration agent, the Strep-Tactin®XT beads can be used again. The Strep-tag® technology stands for the highest protein purities under physiological conditions and can be used in a variety of different applications: in a field of purification, immobilization of proteins for assay development, and for protein interaction studies. More information: https://www.iba-lifesciences.com/stre...