Renilla-luciferin 2-monooxygenase, Renilla luciferase, or RLuc, is a bioluminescent enzyme found in Renilla reniformis, belonging to a group of coelenterazine luciferases.

The Renilla Luciferase Assay System is formulated with a proprietary composition that significantly reduces the effect of coelenterazine autoluminescence compared to other reagents, making the reagent orders of magnitude more sensitive than published methods.

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 .

2023年1月2日 · Renilla luciferase is a popular bioluminescent enzyme, but the molecular details of its mechanism of action on luciferins such as coelenterazine remained elusive.

One of the most common systems is the firefly luciferase-Renilla luciferase enzyme system, where the enzyme activity of Renilla luciferase (encoded by the control plasmid) is used to normalize the firefly luciferase enzyme activity (present on the experimental plasmid).

cell line was created containing a firefly luciferase under the control of the hypoxia-responsive element (HRE) and a constitutively expressed Renillaluciferase reporter.

Renilla Luciferase is a monomeric, 36kDa enzyme that catalyzes the oxidation reaction of the luciferin coelenterazine, using molecular oxygen dissolved in the medium. From: Methods in Enzymology, 2021

2021年5月19日 · Renilla luciferase is an enzyme used as a reporter gene for studying gene regulation and function in vitro and in vivo. In vitro, Renilla luciferase catalyzes the oxidative decarboxylation of coelenterazine (Renilla luciferin) in the presence of O 2 , resulting in the emission of blue light, and the formation of oxyluciferin and CO 2 as the ...

Nature Catalysis | Volume 6 | January 2023 | 23–38 Article CEI CNM CEI i i i –

A protocol for fast, sensitive detection of sea pansy (<em>Renilla reniformis</em>) luciferase. Yield linear results for a concentrations over seven orders of magnitude and reduces coelenterazine autoluminescence commonly seen with other reagents.