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Green
fluorescent protein (GFP) is responsible for the
bioluminescence of the Pacific Northwest jellyfish,
Aequorea victoria. In A.victoria, the 27-kDa
protein absorbs blue light from a photoprotein that is
activated by calcium and emits green light (2). GFP was
isolated from A. victoria and the cDNA was originally cloned
in 1992 by Douglas Prasher (1). Genetic manipulations of GFP
has made it possible for this protein to be expressed in any
organism or cell type(2). GFP expression can be readily
detected in a specimen using an ultra violet light source.
Because GFP expression can be detected in any organism or
cell type, this protein has become a very useful
transgenetic tool. Some applications of GFP include:
determining transcriptional activity of a gene, cell lineage
analyze, development of cell and tissue specific markers,
and tracing the pathways and development of pathogens and
diseases(2).
Embryo transfection is
an useful tool for studying molecular signaling as well as
cell lineages. For example, transfection techniques can be
used to supress signaling by introducing antisense
nucleotides into the embryo or ectopic expression can be
studied by transfecting the embryo with a retrovirus
containing a DNA/cDNA insert of choice. Also,
dominant/negative genes can be introduced to study the
effect of signal interference on cells.
<http://www.plantsci.cam.ac.uk/Haseloff/GFP/GFPbackgrnd.html>
Figure 1. Aequorea victoria emitting green
light.
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