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Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein.The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. [1]
It consists of a modified cell line that has been stably transfected with a DNA construct with a luciferase reporter gene under control of receptor-specific DNA response elements that can stimulate transcription of the inserted luciferase gene and produce the light-generating enzyme which can be easily measured. The DNA response elements can be ...
Firefly luciferase requires D-luciferin to be injected into the subject prior to imaging. The peak emission wavelength is about 560 nm. Due to the attenuation of blue-green light in tissues, the red-shift (compared to the other systems) of this emission makes detection of firefly luciferase much more sensitive in vivo.
The premise behind the test is the activation of downstream reporter gene(s) by the binding of a transcription factor onto an upstream activating sequence (UAS). For two-hybrid screening, the transcription factor is split into two separate fragments, called the DNA-binding domain (DBD or often also abbreviated as BD) and activating domain (AD).
Within the field of molecular biology, a protein-fragment complementation assay, or PCA, is a method for the identification and quantification of protein–protein interactions. In the PCA, the proteins of interest ("bait" and "prey") are each covalently linked to fragments of a third protein (e.g. DHFR, which acts as a "reporter").
ATP is quantified by measuring the light produced through its reaction with the naturally occurring firefly enzyme luciferase using a luminometer. The amount of light produced is directly proportional to the amount of ATP present in the sample. ATP tests can be used to: Control biological treatment reactors; Guide biocide dosing programs