GFP green fluorescent protein

GFP Green fluorescent protein was isolated in jellyfish, Aequorea Victoria. The protein consists of 238 amino acid residues that fluoresce green when exposed to UV light. This method makes it possible to study proteins in their natural environment: the living cell. The gene for GFP was successfully inserted into E. coli bacteria in 1994 and the 2008 Nobel Prize in Chemistry was awarded to Osamu Shimomura, Martin Chalfie and Roger Y. Tsien for Discovery and Development. GFPs.

GFP consists of the side chains of a glycine, a tyrosine and a serine.
Unmodified GFP, wild type (GFP, wGFP) has two maxima of excitation. The first is with a wave length of 395 nm (UV light), the second at 475 nm (blue light). The maximum emission wavelength is 504 nm.
There are now different variants of GFP that have been obtained by modifying it by genetic engineering.
EGFP: green fluorescence (enhanced GFP);
CFP: cyan fluorescence (blue-green), and its Cerulean variant;
EYFP: yellow fluorescence (Y for yellow), and its variants Venus and Citrine;
EBFP: blue fluorescence, and its variant Azurite:
PA-GFP: photo-activatable GFP at 405 nm:
PHluorin: pH-sensitive GFP, turns off at acidic pH.

Other fluorescent proteins

DsRed: red fluorescence, from a coral, of the genus Discosoma. It is at the origin of a second family of variants in the orange-red range.
Keima: red fluorescence with excitation in the blue (important Stokes displacement)
Use in research in biology


The GFP green fluorescent protein can be used as a reporter gene. Associated with a gene of interest, it allows the direct observation of the expression of this gene in the cell with fluorescence microscopy. The gene encoding the GFP protein is incorporated into the genome of the body.
These cells will become fluorescent while those that do not express the gene of interest will remain inert under the light of fluorescence microscopy.

Fluorescence microscopy

Supper-resolution microscopy with two fluorescent proteins (GFP and RFP), associated with Snf2H and H2A genes, Co-localization study in the nucleus of a bone cancer cell.
The discovery of GFP and its derived proteins has profoundly altered fluorescence microscopy and its use in cell biology5. While most small fluorescent molecules, such as fluorescein, are highly toxic when used in living cells, fluorescent proteins such as GFP are much less dangerous when illuminated in the sample.


Mice possessing and expressing the GFP gene under UV light (left and right), compared to a normal mouse (center).
New lines of GFP transgenic rats are being used for gene therapy research, as well as regenerative medicine7. Indeed, most cells labeled with a reporter gene elicit an immune response when introduced into a host. Rat lines expressing high levels of GFP in all their cells could serve as a source of cells to be introduced into another host, which are less likely to cause rejection7. GFP is also widely used in cancer research to mark and track cancer cells. These cells have been used to model metastasis, the process by which cancer cells spread to other organs.

The Use of GFP-Labeling in Fluorescence Microscopy Comprising Fluorescence Resonance Energy Transfer (FRET)

Prior to GFP-labeling, the fluorescent molecules used in fluorescence microscopy were often phototoxic because they harmed living cells by molecular changes when exposed to light. GFP-labeling has allowed living cells to be illuminated without this type of destruction.

Short-term uses of GFP-label in fluorescence microscopy implicated protein being expressed in various structures to increase understanding of differences in cell morphology. The in vivo imaging potential for fluorescence microscopy has been increased by the use of GFP-labeling, leaving for observation of biological processes over time.

FRET technique

FRET is a technique that is used to observe real-time events in a cell. Two variants of GFP that respond to different wavelengths of light through absorption and emission are protein bound.

Tommy Ounas

Tommy Ounas

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