Jellyfish

• In biotechnology
In 1961, Osamu Shimomura of Princeton University extracted green fluorescent protein (GFP) and another bioluminescent protein, called aequorin, from the large and abundant hydromedusa Aequorea victoria, while studying photoproteins that cause bioluminescence by this species of jellyfish. Three decades later, Douglas Prasher, a post-doctoral scientist at Woods Hole Oceanographic Institution, sequenced and cloned the gene for GFP. Martin Chalfie of Columbia University soon figured out how to use GFP as a fluorescent marker of genes inserted into other cells or organisms. Roger Tsien of University of California, San Diego, later chemically manipulated GFP in order to get other colors of fluorescence to use as markers. In 2008, Shimomura, Chalfie, and Tsien won the Nobel Prize in Chemistry for their work with GFP.
Man-made GFP is now commonly used as a fluorescent tag to show which cells or tissues express specific genes. The genetic engineering technique fuses the gene of interest to the GFP gene. The fused DNA is then put into a cell, to generate either a cell line or (via IVF techniques) an entire animal bearing the gene. In the cell or animal, the artificial gene turns on in the same tissues and the same time as the normal gene. But instead of making the normal protein, the gene makes GFP. One can then find out what tissues express that protein—or at what stage of development—by shining light on the animal or cell and observing fluorescence. The fluorescence shows where the gene is expressed.
Jellyfish are also harvested for their collagen, which can be used for a variety of applications including the treatment of rheumatoid arthritis.