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, Dynabeads or multiwell plates. ChromoTek’s GFP-Trap is referenced in more than 1,700 scientific articles and is the gold standard for IP of GFP fusion proteins.
Specificity GFP, EGFP, CFP, YFP, BFP and many more GFP derivatives, see: Fluorescent protein specificity table
Applications Immunoprecipitation (IP) / Co-IP Mass spectrometry (MS) Enzyme activity measurements RIP analysis
Formats/matrices GFP-Trap Agarose GFP-Trap Magnetic Agarose GFP-Trap Dynabeads GFP-Trap Multiwell Plate GFP VHH, recombinant binding protein iST GFP-Trap Kit for IP and MS sample preparation
Synonyms anti-GFP VHH, GFP VHH, GFP-Binding-Protein, GFP Nanobody or anti-GFP single domain antibody (sdAb)
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 1,700 publications 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. GFP-Trap Multiwell Plates for high throughput applications and ELISA iST GFP-Trap kit for immunoprecipitation plussample preparation for mass spectrometry (MS)We offer GFP-Trap as Agarose, Magnetic Agarose, and Dynabeads.
GFP-Trap Agarose GFP-Trap Magnetic Agarose GFP-Trap Dynabeads Low background +++ ++ ++ Binding capacity +++ +++ + Size GFP-tagged protein* Small to large Small to large Small to very large Bead separation centrifugation magnetic magnetic* Does depend on protein size and shape, protein multimers, complexes and interaction partners
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 characterizedThe 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 BFPSee full fluorescent protein specificity list here.
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.
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.
Your GFP-Trap is great! I have never seen such efficient reagent for pulldown.
Prof. Dr. Tomoyuki Tamata University of Dundee
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