Luciferase (firefly recombinant) is a light-generating enzyme that catalyzes an oxidative reaction, using luciferin, ATP, and molecular oxygen to produce oxyluciferin, which yields visible light. The bioluminescence of this ATP-dependent luciferase is commonly used in reporter systems that are amenable to high-throughput screening.
Firefly luciferase is used extensively in molecular and cell biology, in particular for the efficient detection and quantitation of ATP and as a reporter for genetic function.
Luciferase from Photinus pyralis (firefly) has been used as a component of lysis solution to measure luminescence signals, as part of the study to determine chemical signals which can activate the karrikin insensitive 2 (KAI2) pathway.
Firefly luciferase catalyzes the reaction of luciferin with ATP and leads to the production of yellow-green light. The enzyme has a molecular weight of 62kDa and is expressed in peroxisomes. Luciferase is considered as a model to study protein–anesthetic interactions. Firefly luciferase is highly useful in cell biology and molecular biology, as a reporter of gene function and for the quantification of ATP.
Firefly luciferase is a 62 kDa protein that catalyzes the production of light. The enzyme requires ATP, molecular oxygen, and the heterocyclic compound, firefly luciferin, to generate light in a two-step process. The light producing reaction is initiated by luciferin activation (adenylation of its carboxylate group) and proceeds in the presence of molecular oxygen to yield a photon of yellow-green light.
