Flashing lights of luminescent creatures. You see them at dusk on hot summer nights and in pictures from the deepest, darkest parts of the oceans. For many of us they spark memories of magical summer nights. But for scientists they also have sparked ideas and discoveries. Using luciferase, the enzyme that lights up fireflies and other luminescent animals, scientists developed reporter assays that could translate things happening inside cells into a luminescent signal that they could detect and measure. Luminescent assays are used to study cell-signaling pathways and in high-throughput drug discovery assays; they are also used to study the interaction of proteins and in live-cell and in vivo imaging.
With many of these assays, sensitivity and stability are key factors. The more sensitive an assay is, the better the results will be because even low-level changes will be detected. The more stable the reporter is, the more versatile the assay conditions can be. The NanoLuc™ Luciferase (Nluc) offers scientists improvements over existing bioluminescent enzymes in both of these areas.
Only 19.1kDa in size, the monomeric, ATP independent NanoLuc™ Luciferase uses a novel substrate to generate a high-intensity, glow-type luminescence. The enzyme originated in a glowing deep-sea shrimp, and was genetically improved by direct evolution. The stability of the NanoLuc™ Luciferase can reduce compound interference and help with high-throughput screening assays.
The high intensity luminescence of the NanoLuc™ enzyme combined with low autoluminescence of its substrate allows the sensitive detection of low levels of luciferase expression in experimental systems where other forms of luciferase can fail.
Would you like to learn more about you can use this new luciferase technology in your research? Join the Webinar on June 12.
More NanoLuc™ Luciferase Resources
NanoLuc™ Luciferase Overview.