Luciferase has been used as a component in Mix B respiration medium for the determination of the ATP synthetic activity of the H+-ATP synthase. It has also been used in thermal aggregation to assay CnoX (YbbN) activity.
Luciferase may be used:
- to treat mammary tumor cryosections for bioluminescence imaging studies
- as a component of luciferase reaction mixture
- in bioluminescence assay membrane preparations of Zymomonas mobilis
Luciferase from Vibrio fischeri has been used in a study to assess kinetics of light emission and oxygen consumption by bioluminescent bacteria. It has also been used in a study to investigate the sensitivity of dark mutants of various strains of luminescent bacteria to reactive oxygen species.
Alkanal reduced FMN-oxygen oxidoreductase (1-hydroxylating, luminescing)
Luciferase catalyzes the conversion of reduced flavin mononucleotide in the presence of oxygen and long-chain aldehyde to flavin mononucleotide, visible light and a fatty acid. It is a reporter enzyme for sensitive quantitation. The lucifearse fusion proteins have been useful in many protein based interaction studies especially in living cells.
Luciferase (labels HEK293 cells stably expressing pmeLUC；i.p. or intramass injection) can measure the ATP concentration in the tumor microenvironment in real-time in the mouse tumor model inoculated with HEK293 cells stably expressing pmeLUC[1].
Luciferase can clearly monitor the growth of cancer cells in a mouse model in which RENCALUC cells are inoculated subcutaneously[2].
