Photinus-luciferin 4-monooxygenase (LUC) (LUC)

Luciferase refers to a class of oxidative enzymes, most notably from the firefly Photinus pyralis, that catalyze the production of bioluminescence (UniProt P08659). The enzyme facilitates the ATP-dependent oxidation of a substrate, such as D-luciferin, resulting in the emission of light which can be measured with high sensitivity (PubChem CID 16212527). Luciferase is not a therapeutic target for human disease; instead, it serves as a critical reporter gene in biomedical research and drug discovery (PubMed PMID: 17406215). It is widely used to monitor gene expression, evaluate promoter activity, and track protein-protein interactions in cell-based assays. In preclinical studies, luciferase-tagged cells or viruses enable non-invasive bioluminescence imaging (BLI) to observe tumor progression or the distribution of gene therapy vectors in vivo (PubMed PMID: 21938487). While highly effective as a research tool, its use in clinical settings is limited by the potential immunogenicity of the non-human protein and the requirement for exogenous substrate administration.

Other names

Firefly luciferaseLuciferaseBioluminescence reporter genePhotinus pyralis luciferase

Luciferase catalyzes the oxygenation of luciferin in the presence of ATP and Mg2+, producing oxyluciferin, AMP, pyrophosphate, and light emission at approximately 560 nm (PubChem CID 16212527).