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Green Fluorescent Protein, or GFP, was first isolated from the crystal jellyfish Aequorea victoria in the 1960s. In 1994, GFP was successfully cloned<cite>Chalfie1994</cite>, allowing researchers to use the protein as a screenable marker for the first time. Virtually harmless in live cells, GFP has the unique pheotype of glowing bright green under ultraviolet light. GFP functions entirely of its own accord, and requires no exogenous material besides ionizing radiation in order to fluoresce. This allows GFP to be used as a marker accompanying transfected DNA, and has been used extensively in academia. | Green Fluorescent Protein, or GFP, was first isolated from the crystal jellyfish Aequorea victoria in the 1960s. In 1994, GFP was successfully cloned<cite>Chalfie1994</cite>, allowing researchers to use the protein as a screenable marker for the first time. Virtually harmless in live cells, GFP has the unique pheotype of glowing bright green under ultraviolet light. GFP functions entirely of its own accord, and requires no exogenous material besides ionizing radiation in order to fluoresce. This allows GFP to be used as a marker accompanying transfected DNA, and has been used extensively in academia. | ||
In 2011, GFP was used to create an in vivo mammary model to investigate tumorigenesis in mice. Tumor cells were introduced into the mice, accompanied with GFP as a screenable marker. As the mice tumors proliferated, so did GFP. This allowed for easy differentiate between tumors and stroma cells, greatly aiding cancer researchers<cite>Moen2011</cite>. | In 2011, GFP was used to create an in vivo mammary model to investigate tumorigenesis in mice. Tumor cells were introduced into the mice, accompanied with GFP as a screenable marker. As the mice tumors proliferated, so did GFP. This allowed for easy differentiate between tumors and stroma cells, greatly aiding cancer researchers<cite>Moen2011</cite>. | ||
Selectable genetic markers can also be used to investigate protein activity. Research performed at the University of Washington used GFP coupled with inteins to splice GFP into other proteins with greater than 96% efficiency. The GFP proved harmless to the intein's activity, and also allowed the researchers to analyze the effectiveness of the inteins themselves<cite>Ramsden2011</cite>. | |||
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#Zhang2008 [http://www.springerlink.com/content/u2172658q3p50727/ Zhang WJ, Yang SS, Shen XY, Jin YS, Zhao HJ and Wang T] | #Zhang2008 [http://www.springerlink.com/content/u2172658q3p50727/ Zhang WJ, Yang SS, Shen XY, Jin YS, Zhao HJ and Wang T] | ||
//Salt tolerance as a selectable genetic marker. | //Salt tolerance as a selectable genetic marker. | ||
#Ramsden2011 pmid=21708017 | |||
//Use of inteins with GFP to introduce selectable markers into proteins. | |||
</biblio> | </biblio> | ||
