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.

The GFP-Trap® features:

  • a robust and versatile tool for biochemical analyses of GFP-fusion proteins
  • short time incubations (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.
 


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