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

Disclosed are luciferase polypeptides with improved light-emitting activity and their encoding nucleic acids. These molecules are useful in a range of assays including luciferase-based gene reporter assays, bioluminescence resonance energy transfer assays, protein complementation assays and other applications in which luciferase enzymes are utilized as detectable and/or quantifiable labels. Also disclosed are methods and compositions for increasing the sensitivity and/or improving the kinetics of luciferase-catalyzed reactions as well as decreasing the impact of undesirable variables.

Disclosed are luciferase polypeptides with improved light-emitting activity and their encoding nucleic acids. These molecules are useful in a range of assays including luciferase-based gene reporter assays, bioluminescence resonance energy transfer assays, protein complementation assays and other applications in which luciferase enzymes are utilized as detectable and/or quantifiable labels. Also disclosed are methods and compositions for increasing the sensitivity and/or improving the kinetics of luciferase-catalyzed reactions as well as decreasing the impact of undesirable variables.

The present invention relates to a method for assessing cell viability of bacterial and fungal cells and to a method for the detection of bacterial and fungal cells with specific enzyme activities. The methods of the present invention rely on the real-time measurement of the level of luminescence signal from a luciferase enzyme directly from a growing culture of bacterial or fungal cells. Furthermore, the present invention relates to a method for assessing susceptibility of bacterial cells to antibiotics by measuring ATP levels using a luciferase assay system.

The present invention relates to a method for assessing cell viability of bacterial and fungal cells and to a method for the detection of bacterial and fungal cells with specific enzyme activities. The methods of the present invention rely on the real-time measurement of the level of luminescence signal from a luciferase enzyme directly from a growing culture of bacterial or fungal cells. Furthermore, the present invention relates to a method for assessing susceptibility of bacterial cells to antibiotics by measuring ATP levels using a luciferase assay system.

A method to produce novel split-protein sensors are described herein. The method implements a sequence dissimilarity (SD) based design that can identify potential split-sites in proteins to generate a split-protein pair, and then employs structure guided mutagenesis of the fragmented protein interface to generate split-protein sensors. The sensors have a signal to background ratio >200 and can be readily used to monitor protein-protein interactions and their inhibition in cells.

A method to produce novel split-protein sensors are described herein. The method implements a sequence dissimilarity (SD) based design that can identify potential split-sites in proteins to generate a split-protein pair, and then employs structure guided mutagenesis of the fragmented protein interface to generate split-protein sensors. The sensors have a signal to background ratio >200 and can be readily used to monitor protein-protein interactions and their inhibition in cells.

The present invention relates to a fusion protein comprising: —a N-terminal domain which comprises an antibody which is a variable domain of a camelid heavy-chain antibody (VHH) or a single chain variable fragment (scFV) and which is directed against an immunoglobulin and —a C-terminal domain which comprises a polypeptide with a luciferase activity: —having the amino acid sequence SEQ ID NO: 1 or —having at least 80% amino acid sequence identity to the amino acid sequence SEQ ID NO: 1.

A method of treating breast cancer is described, in which a peptide having cancer selective translocation function-doxoribicin conjugate is administered. The conjugate includes doxorubicin chemically linked to the N-terminus or C-terminus of a VEGF-binding protein transduction domain (VPTD) peptide represented as SEQ ID NO: 1, wherein the VPTD peptide and doxorubicin are linked to each other by a disulfide bond, and wherein the VPTD peptide binds specifically to vascular endothelial growth factor (VEGF) in tumor cells or tumor tissues.

A method of treating breast cancer is described, in which a peptide having cancer selective translocation function-doxoribicin conjugate is administered. The conjugate includes doxorubicin chemically linked to the N-terminus or C-terminus of a VEGF-binding protein transduction domain (VPTD) peptide represented as SEQ ID NO: 1, wherein the VPTD peptide and doxorubicin are linked to each other by a disulfide bond, and wherein the VPTD peptide binds specifically to vascular endothelial growth factor (VEGF) in tumor cells or tumor tissues.