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What produces luciferase protein?

What produces luciferase protein?

Luciferase is a light-producing enzyme naturally found in insect fireflies and in luminous marine and terrestrial microorganisms. The firefly enzyme couples the oxidation of luciferin with the energy transfer from ATP and produces yellow–green light with a pH-dependent absorption maximum.

What animals have luciferin?


  • Firefly luciferin is the luciferin found in many Lampyridae species.
  • Coelenterazine is found in radiolarians, ctenophores, cnidarians, squid, brittle stars, copepods, chaetognaths, fish, and shrimp.

How does luciferase assay work?

The luciferase assay is useful to study whether a protein of interest regulates a particular gene at the transcription level. When this protein activates transcription, the cell will produce luciferase enzyme. After the addition of a lysis buffer and a substrate, a luminometer quantifies the luciferase activity.

What is the drug luciferin?

D-luciferin is the substrate for firefly luciferase (Photinus pyralis). The luciferin/luciferase system is used as a very sensitive reporter assay for gene expression. It can also be used for ATP assays in research applications or to detect bacterial contamination.

Can luciferase be tracked?

This is exciting because changes in the luciferase luminescence can be tracked in individual mice (by measuring at multiple time points, e.g. hours, days or weeks), enabling accurate monitoring of dynamic biological processes (such as pregnancy or bacterial infection), and avoiding the need to euthanize numerous mice …

Who named luciferin?

Raphaël Dubois
The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. Both words are derived from the Latin word lucifer, meaning “lightbearer”, which in turn is derived from the Latin words for “light” (lux) and “to bring or carry” (ferre).

What are two main reasons that fireflies glow?

Two chemicals found in their bodies, luciferin and luciferase, spur a reaction in the presence of oxygen, adenosine triphosphate (ATP, which is found in all living things), and other compounds. Luciferin is heat resistant, while luciferase (a bioluminescent enzyme) spurs the emission of light, Harrison explains.

Where is luciferase used?

Luciferases are widely used in biotechnology, for microscopy and as reporter genes, for many of the same applications as fluorescent proteins. However, unlike fluorescent proteins, luciferases do not require an external light source, but do require addition of luciferin, the consumable substrate.

Is luciferase a marker?

Luciferase expression could be monitored in cell extracts in a luminometer. Kinetic experiments in mice proved the suitability of luciferase as an excellent marker for following herpesvirus spread in the animal.

Why is luciferin bad?

Luciferin Toxicity The small size of luciferin also makes it a poor antigen and immune responses to luciferin are unlikely. Luciferin is able to pass the blood brain barrier, the blood placenta barrier and the blood testis barrier, toxicity appears low.

Is luciferase used in medicine?

Luciferase enzymes from a variety of different organisms have been used for BLI studies of viral infection and other biologic processes (Table 1). Firefly (Photinus pyralis) luciferase, optimized for expression in mammalian cells, is the most commonly used luciferase for in vivo imaging.