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J. Lipid Res. 58, 1722–1729. Cell-based, bioluminescent assay for monitoring the interaction between PCSK9 and the LDL receptor. 2017

Duellman, S.J., Machleidt, T., Cali, J.J. and Vidugiriene, J.

Notes: Researchers used NanoLuc® Luciferase technology to monitor the interaction between and LDLR and PCSK9. (4931)

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ACS Chemical Biology 7(11), 1848-57. Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate. 2012

Hall, M.P., Unch, J., Binkowski, B.F., Valley, M.P., Butler, B.L., Wood, M.G., Otto, P., Zimmerman, K., Vidugiris, G., Machleidt, T., Robers, M.B., Benink, H.A., Eggers, C.T., Slater, M.R., Meisenheimer, P.L., Klaubert, D.H., Fan, F., Encell, L.P., and Wood, K.V.

Notes: These authors describe the engineering of an enzyme and substrate to create a novel highly efficient bioluminescence system. The paper introduces NanoLuc™ Luciferase, a small luciferase subunit (19kDa) from the deep-sea shrimp Oplophorus gracilirostris, which provides ∼2.5 millionfold improved luminescence activity in mammalian cells by merging optimization of protein structure with development of a novel imidazopyrazinone substrate (furimazine). The glow-type luminescence (signal half-life >2 hours) produced by the new luciferase has a specific activity ∼150-fold greater than either firefly or Renilla luciferases similarly configured for glow-type assays. In mammalian cells, NanoLuc™ Luciferase shows no evidence of post-translational modifications or subcellular partitioning. The enzyme exhibits high physical stability, retaining activity with incubation up to 55°C or in culture medium for >15 hours at 37°C.
The authors discuss utility of NanoLuc™ Luciferase as a genetic reporter configured for high sensitivity or for response dynamics through addition of a degradation sequence to reduce intracellular accumulation. Data shows the effect of adding a signal sequence to allow export of NanoLuc™ Luciferase to the culture medium, allowing measurement of enzyme activity without cell lysis. (4295)

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