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Both kindling and quenching of wild-type asCP are reversible. Kindled KFP1, on the other hand, relaxes back to a nonfluorescent state with a half-life...
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ANALYTICAL CURRENTS Kindling proteins light a fluorescent “fire” Konstantin Lukyanov and colleagues at the Shemiakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, Evrogen JSC, and Moscow State University (all in Russia) have developed a mutant fluorescing protein that once turned on, stays on. This unique protein can be used for precise, in vivo photolabeling to track the movements of cells, organelles, and other proteins. The mutant, called “kindling fluorescent protein” (KFP1), is based on a wild-type chromoprotein from the sea anemone Anemonia sulcata (asCP). Wild-type asCP fluoresces in response to intense green light irradiation, with an emission peak at 595 nm. The wild-type asCP relaxes back to its initial nonfluorescent state with a half-life of 1.0 

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