Abstract: Luciferase enzymes with greatly increased thermostability, e.g., at least half lives of 2 hours at 50° C., cDNAs encoding the novel luciferases, and hosts transformed to express the luciferases, are disclosed. Methods of producing the luciferases include recursive mutagenesis. The luciferases are used in conventional methods, some employing kits.

Abstract: An object of the present invention is to provide a mutant luciferase having luciferase activity with an altered emission spectrum. A specific amino acid residue(s) is substituted in a luciferase derived from Cypridina noctiluca and then the resulting mutant luciferase having luciferase activity with an emission spectrum differing from that of the wild-type luciferase is screened for.

Abstract: Luciferase enzymes with greatly increased thermostability, e.g., at least half lives of 2 hours at 50° C., cDNAs encoding the novel luciferases, and hosts transformed to express the luciferases, are disclosed. Methods of producing the luciferases include recursive mutagenesis. The luciferases are used in conventional methods, some employing kits.

Abstract: The invention comprises modified luciferase proteins which are more resistant to inhibition by test chemicals than wild type luciferase. The modified luciferases also contain greater thermostability than wild type luciferase.

Abstract: A polynucleotide encoding a modified luciferase polypeptide. The modified luciferase polypeptide has at least 60% amino acid sequence identity to a wild-type Oplophorus luciferase and includes at least one amino acid substitution at a position corresponding to an amino acid in a wild-type Oplophorus luciferase of SEQ ID NO:1. The modified luciferase polypeptide has at least one of enhanced luminescence, enhanced signal stability, and enhanced protein stability relative to the wild-type Oplophorus luciferase.

Abstract: A recombinant protein having luciferase activity and at least 60% similarity to a wild-type luciferase wherein in the sequence of the enzyme, the amino acid residue corresponding to residue 357 in Photinus pyralis luciferase is mutated as compared to the corresponding wild-type luciferase, such that the luciferase enzyme is able to emit light at a different wavelength as compared to the corresponding wild-type luciferase and/or has enhanced thermostability as compared to the corresponding wild-type luciferase. In general, the residue corresponding to 357 in Photinus pyralis luciferase is changed from an acidic amino acid to a non-acidic amino acid and preferably an uncharged polar amino acid such as tyrosine. Mutant luciferases in accordance with the invention can produce a large (50 nm) wavelength shift in emitted light and have good thermostability. The resultant colour shift can be reversed by addition of coenzyme A. These properties make the mutant particularly useful in a variety of assays.

Abstract: The invention provides active, non-naturally occurring mutants of beetle luciferases and DNAs which encode such mutants. A mutant luciferase of the invention differs from the corresponding wild-type luciferase by producing bioluminescence with a wavelength of peak intensity that differs by at least 1 nm from the wavelength of peak intensity of the bioluminescence produced by the wild-type enzyme. The mutant luciferases and DNAs of the invention are employed in various biosensing applications.

Abstract: A protein having luciferase activity and at least 60% similarity to luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata or Luciola lateralis.

Abstract: This invention provides modified nucleotide sequences encoding luciferase that have greater expression than wild type luciferase.

Abstract: The luxA and luxB genes from P. luminescens which encode for the luciferase protein of the bacterial luciferase system were modified to generate codon-optimized versions that are optimized for expression in mammalian cells. The codon-optimized bacterial luciferase enzyme system genes of the invention can be used to develop a mammalian bioluminescence bioreporter useful in various medical research and diagnostics applications.

Abstract: The present invention provides a mutant firefly luciferase consisting of a mutant amino acid sequence derived from the amino acid sequence of a wild-type firefly luciferase by at least substitution (a), (b), or (c) below and having luminescence intensity higher than that of the wild-type firefly luciferase.

Abstract: Provided herein are isolated polynucleotide encoding modified click beetle luciferase polypeptides that have enhanced luminescence and longer wavelength near-infrared signals. The disclosure also relates to near-infrared bioluminescence systems that include said modified click beetle luciferase polypeptides and novel luciferin derivatives, as well as methods of using said modified click beetle luciferase polypeptides and bioluminescence systems.

Abstract: A polynucleotide encoding a secreted form of wild type Renilla luciferase. Also provided is a polynucleotide encoding a secreted modified form of wild type Renilla luciferase. Additionally, the polypeptides encoded by the polynucleotides of the present invention and uses of the polynucleotides and polypeptides of the present invention in biological assays. Also, a stable mammalian packaging cell line which produces retroviruses carrying a polynucleotide encoding a secreted Renilla luciferase.

Abstract: Proteins are provided having luciferase activity with lower Km than wild-type luciferases by altering the amino acid residue at position 270 of the wild-type to an amino acid other than glutamate. Greater heat stability than wild-type luciferases while retaining the lower Km is provided by also replacing the glutamate equivalent to that at position 354 of Photinus pyralis luciferase or 356 of Luciola luciferases with an alternative amino acid, particularly lysine and/or the amino acid residue at 215 of Photinus pyralis and 217 of the Luciola species with a hydrophobic amino acid. DNA, vectors and cells that encode for and express the proteins are also provided as are test kits and reagents for carrying out luminescence assays using the proteins of the invention.

Abstract: Described herein is a variant of wild type Gaussia luciferase that catalyzes glow-type emission kinetics suited for high-throughput functional screening applications. Polypeptides, functional fragments, variants, and nucleic acids that encode the enhanced luciferase are further described. One such polypeptide corresponds to wild type Gaussia luciferase with a substitution mutation of I for M at position 43 of the mature peptide. Methods of use, assay systems and kits that contain the polypeptides and/or nucleic acids are further described.

Abstract: The present invention relates to luciferase having resistance to a surfactant and a method for measuring intracellular ATP which is characterized in that the luciferase having resistance to a surfactant is used in this method comprising the steps of: a first step wherein ATP is extracted from cells in a sample; a second step wherein light emission is produced by adding a luminescence reagent containing luciferase to the extracted ATP solution; and a third step wherein the light emission is measured.

Abstract: The present invention provides a polynucleotide or polynucleotides encoding Oplophorus luciferase which is composed of 19 kDa and 35 kDa proteins, or the 19 kDa photoprotein, the recombinant secretional Oplophorus luciferase or the 19 kDa photoprotein encoded by the polynucleotide(s), an expression vector containing the polynucleotide(s) and a host transformed with the vector. Further, the invention provides a method for producing the recombinant Oplophorus luciferase or the photoprotein. These proteins could be recombinantly produced by culturing the host cell or by in vitro translation system using the recombinant expression vector.

Abstract: Described herein is a variant of wild type Gaussia luciferase that catalyzes glow-type emission kinetics suited for high-throughput functional screening applications. Polypeptides, functional fragments, variants, and nucleic acids that encode the enhanced luciferase are further described. One such polypeptide corresponds to wild type Gaussia luciferase with a substitution mutation of I for M at position 43 of the mature peptide. Methods of use, assay systems and kits that contain the polypeptides and/or nucleic acids are further described.

Abstract: Isolated nucleic acid molecules which code for luciferases able to produce the green bioluminescence of Phrixotrhix vivianii and red bioluminescence of Phrixothrix hirtus are described. The nucleic acid molecules and the luciferases encoded thereby can be used in applications such as diagnostic methods and molecular biology tools.

Abstract: Isolated nucleic acid molecules which code for luciferases able to produce the green bioluminescence of Phrixotrhix vivianii and red bioluminescence of Phrixothrix hirtus are described. The nucleic acid molecules and the luciferases encoded thereby can be used in applications such as diagnostic methods and molecular biology tools.