Our SNAP/CLIP-tag-Trap is a high affinty SNAP-tag and CLIP-tag binding protein coupled to agarose beads for biochemical analysis of SNAP-tag and CLIP-tag fusion proteins and their interacting partners. SNAP- and the CLIP-tag are mutants of the human DNA repair protein O6-alkylguanine-DNA alkyltransferase (hAGT) and are designed to form covalent bonds with with benzylguanine and benzylcytosine derivatives.
- Immunoprecipitation (IP) / Co-IP
- Mass spectrometry
- Enzyme activity measurements
- ChIP/ RIP analysis
- SNAP/CLIP-tag-Trap immunoprecipitates SNAP-tag- and Clip-tag- fusion proteins, no matter if covalently bound to ligands or not
- bound SNAP-tag- and Clip-tag- fusion proteins can be eluted without protease: No need for a protease cleavage site
- SNAP/CLIP-tag-Trap can be used for affinity purification
Immunoprecipitation of SNAP-tag fusion protein with SNAP/CLIP-tag-Trap (left) or an alternative supplier's product (right):
Recombinantly expressed SNAP-tag protein bound to SNAP-Cell TMR-Star™ ligand. Input (I), non-bound (FT) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie blue staining, Western blotting and fluorescence scan. Please note, additional bands are visible due to sensitivity of the SNAP-tag protein to SDS. Apparently, more protein is bound to SNAP/CLIP-tag-Trap compared to competitor's product. Notably, because the SNAP/CLIP-tag-Trap binds to SNAP-tag at an epitope different to the ligand binding site, the SNAP/CLIP-tag-Trap (left) can immunoprecipitate SNAP-tag fusions covalently bound to ligands. In contrast, the competitor's product (right) is significantly less efficient.
With the SNAP/CLIP-tag-Trap, it is possible to pull down SNAP-tag fusion proteins from cells that have been previously treated with SNAP-tag ligands for imaging. It makes the SNAP/CLIP-tag system as versatile as GFP expression, imaging and purification.
Very stable & reliable binding
- high affinity with very low dissociation constant KD of 1.4nM
- harsh washing conditions can be applied
- recombinant, validated antibody
- Structure and function are characterized