The primary transactivation reporter-gene assay screening and the confirmatory transactivation reporter-gene assay utilize a cellular transactivation reporter-gene assay that has been optimized to a 3-day long experiment with 40,000 cells and only 25 of the
luciferases substrates per well, reducing the time and cost of the screening assay.
Recent examples of genetically encoded ATP imaging reagents have utilized
luciferases and fluorescent proteins.
Luciferases are the enzymes that catalyze the light emitting reaction in bioluminescence organisms.
Perhaps the main advance needed to bring these grand notions to fruition is the development of
luciferases that stimulate the emission of a redder light.
Although marine luciferins are well conserved across phyla and often acquired from an organism's diet,
luciferases and photoproteins are encoded in the genes of the luminescent organism itself (reviewed in Haddock et al., 2010).
Expression in Escherichia coli of biotinylated
luciferases using biotin acceptor peptides.
Different enzymes, known collectively as
luciferases, cut luciferin in different places, producing various colors of light.
In the purification of
luciferases A, B, and C (Steps 3-5, below), any side fractions of a target
luciferase that contained a different molecular species were combined with a batch of the corresponding
luciferase species for further purification.
We have isolated two
luciferases that catalyze the luminescent oxidation of coelenterazine.
Bioluminescence is an aerobic oxidation process and the enzyme involved in the production of luminescence is
luciferase. The enzyme catalyzes the oxidation of its substrate, luciferin, and is mediated by a reduced coenzyme, flavin mononucleotide.