Ge Healthcare UK Limited

Ge Healthcare Limited

Amersham Plc

Nigel Paul Michael

Nicholas Thomas

Anne Elizabeth Jones

Simon Lawrence John Stubbs

Valerie Millar

Mark Samuel Jonathan Briggs

Beth Davies

Simon Lawrence Stubbs

Disclosed is a method for increasing the fluorescence of a Cyanine dye molecule comprising at least one NOgroup characterized by the reduction of the at least one NOgroup to NHOH or NHby the action of a nitroreductase. The cyanine dye molecule comprising at least one NOgroup can be used as a substrate for detecting nitroreductase enzyme activity in a composition and allows for the use of a nitroreductase enzyme in an enzyme-reporter system for the detection of analytes, binding reactions or gene expression.

Fluorescent detection method and reagent

The present invention provides novel engineered derivatives of green fluorescent protein (GFP) which have an amino acid sequence which is modified by amino acid substitution compared with the amino acid sequence of wild type Green Fluorescent Protein (SEQ ID NO: 2). The modified GFPs exhibit enhanced fluorescence relative to wtGFP when expressed in non-homologous cells at temperatures above 30&#xb0; C., and when excited at about 490 nm compared to the parent proteins, i.e. wtGFP. An example of a preferred protein is F64L-S175G-E222G-GFP. The modified GFPs provide a means for detecting GFP reporters in mammalian cells at lower levels of expression and/or increased sensitivity relative to wtGFP. This greatly improves the usefulness of fluorescent proteins in studying cellular functions in living cells.

Fluorescent proteins and methods of using same

The present invention provides novel engineered derivatives of green fluorescent protein (GFP) which have an amino acid sequence which is modified by amino acid substitution compared with the amino acid sequence of wild type Green Fluorescent Protein. The modified GFPs exhibit enhanced fluorescence relative to wtGFP when expressed in non-homologous cells at temperatures above 30&#xb0; C., and when excited at about 490 nm compared to the parent proteins, i.e. wtGFP. An example of a preferred protein is F64L-S175G-E222G-GFP. The modified GFPs provide a means for detecting GFP reporters in mammalian cells at lower levels of expression and/or increased sensitivity relative to wtGFP. This greatly improves the usefulness of fluorescent proteins in studying cellular functions in living cells.

Fluorescent proteins

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Amersham, United Kingdom

Nigel Paul Michael