Abstract: According to one embodiment, the present invention relates to luciferase derived from Malaysian Luciola firefly, the luciferase having a maximum luminescent wavelength of 580 nm at pH 8, or the luciferase indicating 23.3 times or more of luminescent intensity in comparison to that of Rhodamine 6G.

Abstract: This invention provides a genetically modified marine luciferase such as Gaussia luciferase, which has high bioluminescence intensity, and has high bioluminescence stability and/or red-shifted wavelength. Specifically disclosed is a luciferase variant with improved optical property obtained by replacing at least one amino acid residue among the amino acid sequence of a marine luciferase at positions corresponding to positions 89 to 118 in the amino acid sequence of Gaussia luciferase (GLuc), wherein an amino acid residue at a position corresponding to at least one selected from positions 89, 90, 95, 97, 100, 108, 112, 115, and 118 in the amino acid sequence of GLuc is replaced by way of conservative amino acid replacement. The above-mentioned replacement in a marine luciferase improves enzymatic activity of the luciferase. Also disclosed is a bioluminescent probe having an improved optical property, which is produced using the luciferase variant of the present invention.

Abstract: A novel luciferase that distinct from conventional luciferase has been desired. A luciferase mutant comprising the amino acid sequence of SEQ ID NO: 2 substituted at tyrosine at the position of 138, and at least 3 positions selected from the group consisting of isoleucine at the position of 90, proline at the position of 115, glutamine at the position of 124, and asparagine at the position of 166.

Abstract: Proteins are provided having luciferase activity with greater heat stability than wildtype luciferases by 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. 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. Preferred proteins have a second replaced amino acid at a position equivalent to position 215 of Photinus pyralis luciferase or 217 of Luciola luciferases.

Abstract: Disclosed is a purified luciferase and a method for making it. The luciferase is obtained from Luciola cruciata. The luciferase has a pH range for stabililty of 6.5-9.0 and a optimum pH range of 8.0-9.5. The enzyme does not act on ADP, CTP, UTP and GTP.

Abstract: A codon optimized and stabilized luciferase gene and a novel recombinant DNA characterized by incorporating this new gene coding for a novel luciferase into a vector DNA for improved activities in mammalian cells, are disclosed. This new luciferase exhibits long-wavelength light emission, as well as improved thermostability and higher expression levels in mammalian cell systems, compared to native luciferase. Assays using this new enzyme for measuring various biological metabolic functions are described.

Abstract: A novel luciferase that is distinct from conventional luciferase has been desired. A luciferase mutant comprising an amino acid sequence in which glutamic acid at position 4, arginine at position 11, leucine at position 18 and valine at position 27 are substituted with other amino acids, in the amino acid sequence of SEQ ID NO: 2.

Abstract: This invention relates to: the development of a mutant firefly luciferase in order to use dATP as a DNA polymerase substrate upon pyrosequencing, such luciferase being subjected to substrate specificity modification in a manner such that the dATP-induced activity alone is decreased while the ATP-induced activity is maintained; and a mutant firefly luciferase for which the proportion of activity induced by dATP to activity induced by ATP (dATP/ATP) is lower than that for the wild-type firefly luciferase, in which an amino acid identified based on homology analysis as corresponding with the 421st amino acid (glycine) of the amino acid sequence of the wild-type North American firefly (Photinus pyralis) luciferase has been substituted with a polar amino acid.

Abstract: A modified luciferase protein which is a sensor for molecules including cAMP, cGMP, calcium, chelators thereof, kinases, or phosphatases is provided. Also provided is a circularly permuted anthozoan luciferase protein and a decapod crustacean luciferase protein, optionally containing one or more heterologous amino acid sequences, at least one of which directly or indirectly interacts with a molecule of interest. Further provided is a modified anthozoan luciferase protein and a decapod crustacean luciferase protein containing an insertion of one or more heterologous amino acid sequences, at least one of which directly or indirectly interacts with a molecule of interest.

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: Use of a luciferase that has a mutation of at least one amino acid selected from the group consisting of positions 14, 35, 182, 232 and 465, where the numbering is according to the sequence of the luciferase from P. pyralis (SEQ ID NO:1) in a method that is performed at a pH below the optimal pH for the wild-type luciferase during at least part of the time period over which bioluminescence measurements are taken, wherein the specific activity of the mutant luciferase is higher than the specific activity of wild-type at the pH at which the method is carried out.

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

Abstract: The present invention provides genes encoding novel luciferases having at least the properties of: being capable of using coelenterazine as their luminescent substrates; and being capable of being recombinantly expressed in a mammal cell as a host and produced to be secreted to the outside of the host cell. Specifically, the gene encoding novel luciferases according to the present invention is a DNA molecule comprising a nucleotide sequence encoding any of the full-length amino acid sequences of two types of luciferase proteins, luciferase 1 and luciferase 2, from M. pacifica, and is, for example, a gene encoding the following full-length amino acid sequence of the luciferase 1.

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: Nucleotide and amino acid sequences of luciferase peptides that are encoded by genes within the genome of Arachnocampa (Diptera) are disclosed. Specifically provided are functional ATP-dependent luciferases that catalyze luminescence reactions with emission spectra within the blue portion of the spectrum. The present invention specifically provides isolated peptide and nucleic acid molecules, methods of identifying orthologs and active subsequences of the enzyme peptides, and methods of identifying modulators and substrates of the luciferase peptides. Methods of assays, including multiple reporter assays utilizing at least two ATP-dependent luciferases are provided.

Abstract: This invention relates to: the development of a mutant firefly luciferase in order to use dATP as a DNA polymerase substrate upon pyrosequencing, such luciferase being subjected to substrate specificity modification in a manner such that the dATP-induced activity alone is decreased while the ATP-induced activity is maintained; and a mutant firefly luciferase for which the proportion of activity induced by dATP to activity induced by ATP (dATP/ATP) is lower than that for the wild-type firefly luciferase, in which an amino acid identified based on homology analysis as corresponding with the 421st amino acid (glycine) of the amino acid sequence of the wild-type North American firefly (Photinus pyralis) luciferase has been substituted with a polar amino acid.

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.

Abstract: Provided are methods and compositions useful in detecting protease activity in a sample, as well as methods of identifying agents that modulate protease activity. The methods and compositions provide a modified luciferase polynucleotide sequence and a luciferase polypeptide containing protease recognition sequences, wherein cleavage of the recognition sequence by a protease inhibits luciferase activity. Further provided are methods and compositions for detecting and modulating caspase activity and apoptosis.

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: 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.