What is pRL TK?
The thymidine kinase promoter-Renilla luciferase reporter plasmid (pRL-TK) is commonly used as a control for transfection efficiency in the Dual-Luciferase Reporter Assay System.
What is Renilla luciferase?
Renilla luciferase is an enzyme that catalyzes the chemical reaction which is responsible for the green bioluminescence of Renilla reniformis, a soft coral also known as sea pansy and a member of the class Anthozoa [1].
What is dual luciferase reporter assay?
The Dual-Luciferase® Reporter (DLR™) Assay System provides an efficient means of performing two reporter assays. In the DLR™ Assay, the activities of firefly (Photinus pyralis) and Renilla (Renilla reniformis or sea pansy) luciferases are measured sequentially from a single sample.
Who named luciferase?
Raphaël Dubois
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.
What is luciferase assay used for?
A luciferase assay is used to determine if a protein can activate or repress the expression of a target gene.
Where is luciferase located?
Luciferase is a light-producing enzyme naturally found in insect fireflies and in luminous marine and terrestrial microorganisms.
How is luciferase detected?
In the luciferase reaction, light is emitted when luciferase acts on the appropriate luciferin substrate. Photon emission can be detected by light sensitive apparatus such as a luminometer or modified optical microscopes. This allows observation of biological processes.
Where is luciferase made?
How long has luciferase been used?
While DuBois discovered the reaction between luciferin and luciferase in 1885, it was not until the late 1940s when the luciferase protein was first extracted and purified firefly lanterns by Drs. Green and McElroy. Using this process, they isolated the enzyme and determined its conformational structure.