Luciferase Firefly, Active

Source: Escherichia Coli.Sterile Filtered colorless solution.Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-311 a.a) and having a molecular mass of 38.5kDa. Luciferase is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Protein function: Upon binding the substrate, the enzyme catalyzes an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO(2) molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light. [The UniProt Consortium]