TCO-PEG4 Twin Strep-tag II Peptide contains two copies of the eight-residue Strep-tag II sequence WSHPQFEK separated by PEG-like spacers and a central cysteine used for site-selective conjugation. Strep-tag II Affinity Peptide Strep-tag II is a compact affinity tag engineered to bind streptavidin-derived affinity reagents such as Strep-Tactin. Its small size and defined eight-amino-acid sequence make it useful for purification, detection, immobilization, and interaction studies involving tagged proteins. The Strep-tag system is valued for mild affinity purification conditions and for the ability to use the tag at either protein terminus or in engineered fusion constructs. Tandem / Twin Strep-Tag Concept Using two Strep-tag II motifs in one construct increases multivalent interaction with engineered streptavidin reagents. LT8690 contains two WSHPQFEK motifs separated by PEG-like spacer regions, providing spatial separation between the affinity tags. TCO-PEG4 Functionalization The central cysteine is configured for maleimide coupling to a TCO-PEG4 reagent. Trans-cyclooctene (TCO) can react rapidly with tetrazines through inverse-electron-demand Diels-Alder chemistry, enabling bioorthogonal conjugation strategies. - Affinity capture and detection
- Protein immobilization
- Strep-Tactin binding studies
- Tetrazine-TCO click chemistry
- Surface functionalization
- Multivalent tag research
References Schmidt TGM, Skerra A. The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat Protoc. 2007;2:1528-1535.
doi: 10.1038/nprot.2007.209.
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