The ChromoTek GFP-Trap® is a ready to use affinity resin for immunoprecipitation (IP) of GFP-fusion proteins.

GFP-Trap consists of an anti-GFP Nanobody/ VHH coupled to agarose or magnetic agarose beads. ChromoTek’s GFP-Trap is referenced in more than 1,600 scientific articles and is the gold standard for IP of GFP fusion proteins.

GFP, EGFP, CFP, YFP, BFP and many more GFP derivatives, see:
Fluorescent protein specificity table

Immunoprecipitation (IP) / Co-IP
Mass spectrometry (MS)
Enzyme activity measurements
RIP analysis

GFP-Trap Agarose
GFP-Trap Magnetic Agarose
GFP VHH, recombinant binding protein
iST GFP-Trap Kit

anti-GFP VHH, GFP VHH, GFP-Binding-Protein, GFP Nanobody or anti-GFP single domain antibody (sdAb)

Benefit from GFP-Trap for Immunoprecipitation (IP)

  • Effective pulldown of GFP-fusion proteins for consistent results
  • No heavy & light antibody chains, short incubation (5-30 min)
  • Extraordinary binding, also under harsh conditions
  • Very high affinity (KD=1 pM) to bind even low abundant proteins
  • Reliable gold standard with more than 1,500 publications

Format/matrices & properties

We offer GFP-Trap as Agarose, Magnetic Agarose, and uncoupled as purified protein.

  GFP-Trap Agarose GFP-Trap Magnetic Agarose
matrix agarose magnetic agarose
color white black
particle size 90 µm 40 µm
binding capacity 12 µg/ 10 µl 8 µg/ 10 µl
magnetic no yes
may be centrifuged up to 2,500 x g 800 x g

Extraordinary stable & reliable binding

  • Dissociation constant KD of 1 pM
  • Stable up to 80°C, 1 mM DTT, 3 M Guanidinium•HCl, 8 M Urea, 2 M NaCl, 2 % Nonidet P40 Substitute, 1 % SDS, 1 % Triton X-100
  • Fulfills highest requirements for antibody validation
  • Structure and function are characterized


The GFP-Trap® specifically binds to most common GFP derivatives:

  • AcGFP, Clover, eGFP, Emerald, GFP, GFP5, GFP Envy, GFP S65T, mGFP, mPhluorin, PA-GFP, Superfolder GFP, TagGFP, TagGFP2, monomeric eGFP A206K
  • CFP
  • YFP, Citrine, eCitrine, eYFP, Venus, Ypet
  • BFP

See full fluorescent protein specificity list here.

About GFP

Green Fluorescent Protein (GFP) was first isolated from the jellyfish Aequorea victoria in 1962 by Osamu Shimomura. 30 years later, Douglas Prasher eventually managed to clone the sequence of GFP and Martin Chalfie expressed this sequence in vivo. Later, the work of Roger Tsien’s lab led to the development of the research tool(s) GFP. Simomura, Chalfie, and Tsien were awarded the Nobel Prize in 2008.
Scientists developed many GFP variants with different functional and spectral properties. The first significant improvement of GFP was mutation S65T, which increased intensity and stability of the fluorescence signal. The main excitation peak has been shifted to 488 nm (Heim et al., 1995). EGFP is an engineered version of GFP, which facilitates the practical use of GFP in a variety of different organisms and cells.

GFP-Trap is the gold standard

The best anti-GFP antibody for immunoprecipitation: GFP-Trap

Our customers published more than 1,500 scientific articles referencing GFP-Trap. That’s awesome! The GFP-Trap is the most frequently cited monoclonal anti-GFP antibody and the gold standard for immunoprecipitation of GFP-fusion proteins.

When ChromoTek introduced the GFP-Trap back in 2008, it pioneered the use of GFP-fusion proteins: For the first time, their effective pull-down was possible. Today, scientists apply GFP-Trap in a multitude of experiments for GFP-tagged proteins because of its outstanding performance.



Customer feedback

"Your GFP-Trap is great! I have never seen such efficient reagent for pulldown."

Prof. Dr. Tomoyuki Tamata
University of Dundee

Download Whitepaper
Order Free Test-Sample
Email newsletter

Only for research applications, not for diagnostic or therapeutic use!