High performance research tools
and protein isolation
proprietary Strep-tag® technology
exploits one of the strongest non-covalent interactions in nature: the
interaction of biotin and streptavidin. The system is based on the highly
selective and easily controllable interaction between the synthetic Strep-tag®II
peptide and the specially engineered streptavidin, called Strep-Tactin®,
which is one of the most stable proteins known. The Strep-tag®II
binds specifically to the engineered streptavidins,
by occupying the binding pocket of the natural ligand biotin. Hence, the
interaction is easily reversible by excessive addition of the competitor.
affinity tags – two streptavidin derivatives: The Strep-tag®II
consists of eight amino acids (Trp-Ser-His-Pro-Gln-Phe-Glu-Lys),
whereas the Twin-Strep-tag® includes
this motif two times in series connected by a linker and is accordingly
composed of 28 amino acids. Both exhibit intrinsic, although unequal, affinity
towards the streptavidin derivative Strep-Tactin® and
its successor Strep-Tactin®XT:
The binding affinity of Strep-tag®II
to Strep-Tactin® (1µM)
is nearly 100 times higher than to streptavidin. A further improvement was
achieved by the development of Strep-Tactin®XT,
which shares a nM
affinity with the Strep-tag®II
and a pM
affinity with the Twin-Strep-tag®.
a result of the differences in binding strength among the possible tag-ligand
combinations, the Strep-tag® system
has become established as a universal tool for isolation of proteins, cells,
•Fused to recombinant proteins,
or Twin-Strep-tag® enable
efficient one-step purification on immobilized Strep-Tactin® or
•When fused to antibody-derived
Fab fragments or nanobodies, Twin-Strep-tag® binds
to multimerized Strep-Tactin® allowing
capturing and releasing of target cells and exosomes based on their
surface-marker or antigen-specificity.
on its turn, can be conjugated to microplates, fluorophores or chips, allowing
a wide range of analytical applications after isolation of target material,
such as detection, immobilization and interaction studies.
Learn more about Strep-tag® technology
for your target material of interest:
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