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Experimental note (Bioimaging)

Recombinant Green Fluorescent Protein Derivatives as a Fusion Tag for in vitro Experiments
Chang-Hun Lee1,*
1Department of Biological Chemistry, Johns Hopkins University, School of Medicine
*Corresponding author
  Received : March 24, 2009
  Accepted : March 27, 2009
  Published : March 27, 2009
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Synopsis

In biochemistry and molecular biology, fusion protein technique allows us to isolate a protein of interest with easier purification methods or to identify the tagged protein even when any antibody of the target protein is yet developed. Green fluorescent protein (GFP) and its derivatives have been used as a fusion tag for many proteins in living cells and many in vivo experiments due to its convenience of non-invasive monitoring. Likewise, fluorescent proteins can be advantageous when they are being used as fusion tag for recombinant proteins in vitro. This paper introduces the approaches to take advantage of GFP variants as a fusion tag for in vitro experiments.

Keyword: Green fluorescent protein (GFP), Protein purification, fusion tag, in vitro assay, protein binding assay, recombinant protein, protein expression, Bi-molecular fluorescent complementation, FRET, Biofluorescence
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