Promega launches novel luciferase more versatile than current bioluminescent enzyme

Promega Corporation announces the launch of a novel luciferase that is smaller, brighter, and more versatile than any current bioluminescent enzyme. These attributes of the NanoLuc Luciferase provide new capabilities in reporter assays with potential in biologically complex applications that require greater sensitivity.

NanoLuc technology includes a novel substrate, furimazine, developed by Promega organic chemists and a unique enzyme developed by Promega research scientists using directed evolution techniques. It has unparalleled small size allowing for enhanced viral delivery and protein fusion applications, and it is easily secreted from cells. The enzyme is two orders of magnitude brighter than either firefly (Photinus pyralis) or Renilla reniformis luciferases resulting in better performance in hard to transfect cells. Also, NanoLuc performs in more physiologically relevant models including complex biological samples. With add and measure simplicity and a stable signal, NanoLuc Luciferase can be scaled from bench-top to high-throughput screening applications with no modifications.

To meet the many application needs in a 'next-gen' genetic reporter, 12 plasmid versions of NanoLuc Luciferase are available. The offerings include NanoLuc-PEST (NlucP), which closely couples protein expression to changes in transcriptional activity and increased signal-to-background ratios. For a secreted reporter, a NanoLuc Luciferase construct has been prepared by fusion to an N-terminal secretion signal (secNluc). Using the Nano-Glo^™ Luciferase Assay Reagent, luminescence is linear over a 1,000,000-fold concentration range with a signal half-life ≥2 hours.