The GFP-Trap® for functional and biochemical studies of fluorescent proteins

The green fluorescent protein (GFP) was originally isolated from the jellyfish Aequora victoria. GFP absorbs blue light and emits green light with an emission peak of ~ 509 nm.
In molecular and cell biology green fluorescent proteins and spectral derivates thereof are the most popular tools to study gene expression, protein localization and dynamics in vivo.

With the GFP-Trap® we offer a high quality, single domain GFP-binding protein coupled to a monovalent matrix for biochemical studies (Pulldown, Immunoprecipitation, Co-IP, Western Blot, Mass spec or ChIP) of your fluorescent fusion proteins and their interacting partners.

The GFP-Trap® features:

  • a robust and versatile tool for biochemical analyses of GFP-fusion proteins
  • short incubation times (5 – 30 min)
  • quantitative isolation of fusion proteins and transiently bound factors from
    various cell extracts and organelles (from all organisms)
  • no unspecific binding or contamination by heavy and light chains of conventional antibodies
  • functionality for Chromatin Immunoprecipitation (ChIP)
Comparison of GFP-Trap®_A and GFP-Trap®_M

Left (IP): Pulldown of GFP with GFP-Trap®_A and GFP-Trap®_M from 293T cell extracts. Input (I) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining.
Right (Co-IP): Pulldown of GFP-PCNA with GFP-Trap®_A and GFP-Trap®_M from 293T cell extracts. Other bands: potential interaction partners of PCNA.
Comparison of GFP-Trap® with conventional
mono- and poly-clonal antibodies

Immunoprecipitations (IP) of GFP from protein extracts of GFP-producing human cells. Input (I), non-bound (FT) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining and Western Blotting. (hc) heavy chain, (lc) light chain of conventional antibodies.

GFP-multiTrap®

Now you can take advantage of the proven efficiency of our GFP-Trap® in a convenient 96-multiwell format.

As the GFP-Trap® is immobilized in the wells no centrifugation is necessary and you can easily test your GFP fusion proteins for peptide, protein, DNA or RNA binding.

Rapidly quantify your input, wash and bound fractions of GFP fusion proteins and fluorescently labeled binding substrates with fluorescence scanners and plate readers.

GFP-Booster for "Nanoscopy"

GFP signal intensities at physiological expression levels are usually too low for super-resolution microscopy.

ChromoTek's GFP-Booster enables you now to use your existing expression constructs and cell lines also for super-resolution microscopy. With our GFP-Booster it was now for the first time possible to study the protein machinery involved in the abszission process, the last step of cell division.
The fluorescence enhancement by the GFP-Booster enabled super-resolution microscopy to resolve the 3D distribution of GFP-tagged proteins and provided novel insights into the cell division process.
(Guizetti et al., 2011, Science, Feb. 10, Epub, PubMed)

 


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