Patents by Inventor Laurence C. Tisi

Laurence C. Tisi has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).

  • MUTANT LUCIFERASE
    Publication number: 20140170686
    Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Phtotinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the seguence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.
    Type: Application
    Filed: January 17, 2014
    Publication date: June 19, 2014
    Applicant: Promega Corporation
    Inventors: David J. Squirrell, Melenie J. Murphy, Rachel L. Price, Christopher R. Lowe, Peter J. White, Laurence C. Tisi, James A. H. Murray
  • MUTANT LUCIFERASE
    Publication number: 20140170687
    Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the sequence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.
    Type: Application
    Filed: January 17, 2014
    Publication date: June 19, 2014
    Applicant: PROMEGA CORPORATION
    Inventors: David J. Squirrell, Melenie J. Murphy, Rachel L. Price, Christopher R. Lowe, Peter J. White, Laurence C. Tisi, James A. H. Murray
  • Mutant luciferase
    Patent number: 8652794
    Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the sequence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.
    Type: Grant
    Filed: February 9, 2011
    Date of Patent: February 18, 2014
    Assignee: Promega Corporation
    Inventors: David J. Squirrell, Melenie J. Murphy, Rachel L. Price, Christopher R. Lowe, Peter J. White, Laurence C. Tisi, James A. H. Murray
  • MUTANT LUCIFERASE
    Publication number: 20110177540
    Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the sequence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.
    Type: Application
    Filed: February 9, 2011
    Publication date: July 21, 2011
    Inventors: David J. Squirrell, Melenie J. Murphy, Rachel L. Price, Christopher R. Lowe, Peter J. White, Laurence C. Tisi, James A. H. Murray
  • Thermostable luciferase mutant
    Patent number: 7906298
    Abstract: A protein having luciferase activity and at least 60% similarity to luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata or Luciola lateralis.
    Type: Grant
    Filed: October 26, 1999
    Date of Patent: March 15, 2011
    Assignee: Promega Corporation
    Inventors: David J Squirrell, Melenie J Murphy, Rachel L Price, Christopher R Lowe, Peter J White, Laurence C Tisi, James A H Murray
  • Method for determining the amount of template nucleic acid present in a sample
    Patent number: 7371545
    Abstract: A method for determining the amount of template nucleic acid present in a sample comprising the steps of: I) bringing into association with the sample all the components necessary for nucleic acid amplification, and all the components necessary for a bioluminescence assay for nucleic acid amplification and subsequently: ii) performing the nucleic acid amplification, iii) monitoring the intensity of light output from the bioluminescence assay; and iv) determining the amount of template nucleic acid present in the sample.
    Type: Grant
    Filed: January 14, 2004
    Date of Patent: May 13, 2008
    Assignee: Lumora Limited
    Inventors: Laurence C. Tisi, James A. H. Murray