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 beads, magnetic agarose beads or Dynabeads. 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
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
What GFP-Trap shall I use?
- GFP-Trap Agarose, when lowest background and high binding capacity IP is needed.
- GFP-Trap Magnetic Agarose, when magnetic separation and high binding capacity IP is needed.
- GFP-Trap Dynabeads, when very large proteins/complexes are investigated, and magnetic separation is needed for IP.
Comparison of matrices & properties
We offer GFP-Trap as Agarose, Magnetic Agarose, and Dynabeads.
|GFP-Trap Agarose||GFP-Trap Magnetic Agarose||GFP-Trap Dynabeads|
|Size GFP-tagged protein*||Small to large||Small to large||Small to very large|
* Does depend on protein size and shape, protein multimers, complexes and interaction partners
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 (GFP-Trap Dynabeads: 10mM DTT, 0,2% SDS)
- 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
- YFP, Citrine, eCitrine, eYFP, Venus, Ypet
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.
Application notes & white papers
- Capture Surface for Biacore assays
- Chromatin Immunoprecipitation (ChIP) Protocol for A. thaliana
- Elution of GFP-fusion protein from the GFP-Trap
- GST- & GFP- nanobodies for bead-based protein arrays e.g. Luminex®
- On-bead digest protocol for mass spectrometry
- On-bead enzyme assay
- Ubiquitination of GFP-tagged proteins
"Your GFP-Trap is great! I have never seen such efficient reagent for pulldown."
Prof. Dr. Tomoyuki Tamata
University of Dundee
Only for research applications, not for diagnostic or therapeutic use!