NanoLuc luciferase (Nluc)

NanoLuc luciferase is an engineered 19 kDa enzyme derived from the luciferase of the deep-sea shrimp Oplophorus gracilirostris. It was specifically designed for high physical stability and intense bioluminescence, producing approximately 150 times more light than traditional Firefly or Renilla luciferases when using its optimized substrate, furimazine (Hall et al., 2012). The enzyme functions as an oxidoreductase, catalyzing the oxidation of furimazine to produce a high-intensity blue light emission at 460 nm (England et al., 2016). Due to its small size and high thermal stability, it is widely utilized as a reporter gene in molecular biology to study gene expression, protein-protein interactions via Bioluminescence Resonance Energy Transfer (BRET), and protein stability (Promega, 2024). While NanoLuc is not a therapeutic target for treating human disease, it is an essential tool in drug discovery for high-throughput screening and in vivo imaging of pathogens or tumor progression (Dixon et al., 2016). Its use in vivo is primarily limited to research models, as the enzyme is non-human and may elicit an immune response if introduced into patients (Stacer et al., 2013).

Other names

NanoLucNluc19kDa Oplophorus luciferase variantOplophorus-derived luciferaseOluc variant

NanoLuc luciferase catalyzes the oxidative decarboxylation of the substrate furimazine in the presence of molecular oxygen to produce high-intensity blue light (460 nm), carbon dioxide, and furimamide (Hall et al., 2012).