More than 700 peer reviewed publications have cited use of the GFP-trap.
Try it yourself and find out just why it's so popular!

ChromoTek nanobodies are small, recombinant antigen binding fragments derived from the V_HH domain of the alpaca antibody.

Bound to agarose or magnetic beads, nanobodies form a nano-trap - an elegantly simple reagent that makes immunoprecipitation fast, clean, and easy.

Nano-traps like the GFP-trap and RFP-trap are better tools for IP than traditional monoclonal or polyclonal antibodies, because they are:

• Cleaner: Heavy and light chain contamination are always problematic concerns in an IP - nanotraps have neither a heavy nor a light chain, and contain only the fragment of the antibody necessary for antigen binding
• Faster:  A nano-trap immunoprecipitation can be completed in just one hour (less than one-third the time required for a traditional antibody IP)
• More Consistent & Reproducible: Recombinantly produced nano-traps don't suffer from cell line drift, or the batch specific variance issues commonly associated with monoclonal or polyclonal antibodies
• Better Binders: Nano-traps have exceptionally high affinity constants. The RFP-trap and GFP-trap boast respective 5 nanomolar and 1 picomolar dissociation constants!
• More Efficient: Smaller size and higher affinity means that significantly more protein can be bound per uL of GFP or RFP-trap slurry (when compared to conventional mono or polyclonal antibodies)