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Biophys. J. 75, 2205-2211. Structural basis for the inhibition of firefly luciferase by a general anesthetic. 1998

Franks, N.P., Jenkins, A., Conti, E., Lieb, W.R., Brick, P.

Notes: QuantiLum™ Recombinant Luciferase was used to study the inhibition of luciferase activity by the general anesthetic, bromoform. The competition mechanism was confirmed by solving the crystal structure of luciferase with bound bromoform. (1171)

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EMBO J. 16, 659-671. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. 1997

Lee, G. J. , Roseman, A. M. , Saibil, H. R. , Vierling, E.

Notes: The Quantilum™ Recombinant Luciferase was heat denatured in the presence of heat shock protein hsp 18.1 and the renaturation of the protein was assayed in with the Luciferase Assay System. The denaturation was performed in either Rabbit Reticulocyte Lysate or Wheat Germ Extract in the presence or absence of added ATP. (0809)

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Luciferase Assay System

QuantiLum® Recombinant Luciferase

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