In one embodiment, an object of the present invention is to provide a liquid cycling luminescence reagent excellent in stability. In one embodiment, the present invention provides a liquid composition for measuring ATP and AMP and/or ADP in a sample after storage of the liquid composition, wherein (i) the liquid composition comprises luciferase, luciferin, an enzyme that catalyzes a reaction that produces ATP from AMP, a substrate of the enzyme that catalyzes a reaction that produces ATP from AMP, and a cofactor, or when at least one of these components is not contained in the liquid composition, the component that is not contained in the liquid composition is added to the liquid composition before or during measurement, and (ii) the relative luminescence level of the liquid composition during storage is 5500 RLU or less, and the relative level of luminescence is a value determined by subtracting a control value from a measurement value.

In one embodiment, an object of the present invention is to provide a liquid cycling luminescence reagent excellent in stability. In one embodiment, the present invention provides a liquid composition for measuring ATP and AMP and/or ADP in a sample after storage of the liquid composition, wherein (i) the liquid composition comprises luciferase, luciferin, an enzyme that catalyzes a reaction that produces ATP from AMP, a substrate of the enzyme that catalyzes a reaction that produces ATP from AMP, and a cofactor, or when at least one of these components is not contained in the liquid composition, the component that is not contained in the liquid composition is added to the liquid composition before or during measurement, and (ii) the relative luminescence level of the liquid composition during storage is 5500 RLU or less, and the relative level of luminescence is a value determined by subtracting a control value from a measurement value.

Screening methods as well as kits for identifying modulators of hydroxysteroid (17-beta) dehydrogenase (HSD17B) family member proteins, such as HSD17B13, are provided. The methods comprise screening molecules for their capacity to modulate the HSD17B family member protein, including inhibiting the HSD17B family member protein, as measured by substrate depletion, product concentration from the HSD17B family member protein substrate conversion or NADH concentration, levels of labeled substrate, luciferin light emission, or combinations thereof. Inhibitors of HSD17B family member proteins identified through the screening methods may be used to treat liver diseases, disorders, or conditions in which the HSD17B family member protein plays a role.

Screening methods as well as kits for identifying modulators of hydroxysteroid (17-beta) dehydrogenase (HSD17B) family member proteins, such as HSD17B13, are provided. The methods comprise screening molecules for their capacity to modulate the HSD17B family member protein, including inhibiting the HSD17B family member protein, as measured by substrate depletion, product concentration from the HSD17B family member protein substrate conversion or NADH concentration, levels of labeled substrate, luciferin light emission, or combinations thereof. Inhibitors of HSD17B family member proteins identified through the screening methods may be used to treat liver diseases, disorders, or conditions in which the HSD17B family member protein plays a role.

A technique for predicting the presence or absence of an aroma property or an olfactory receptor activation property in a substance is provided. The presence or absence of the objective property is predicted for a test substance on the basis of the maximum similarity of stereochemical structure between the test substance and a reference substance.

A detection method of a target molecule in a specimen includes a (target molecule)-(labeled binding molecule)-(capturing molecule) complex forming step of reacting the target molecule in the specimen, a capturing molecule that binds to the target molecule, and a labeled binding molecule that binds to the target molecule and which is labeled with an enzyme that catalyzes a reaction to produce ATP, to form a complex formed of the target molecule, the capturing molecule, and the labeled binding molecule, a step of removing the labeled binding molecules which did not bind to the target molecule, an ATP production step of producing ATP by reacting the (target molecule)-(labeled binding molecule)-(capturing molecule) complex with a substrate of the enzyme that catalyzes a reaction to produce ATP, an ATP amplification step of amplifying the produced ATP, and an ATP detection step of detecting the amplified ATP.

Disclosed herein are methods and systems for rapid detection of microorganisms such as bacteria in a sample. A genetically modified bacteriophage is also disclosed which comprises an indicator gene encoding one subunit of an indicator protein. The specificity of the bacteriophage allows detection of a particular bacteria of interest and an indicator signal may be amplified to optimize assay sensitivity.

Disclosed herein are methods and systems for rapid detection of microorganisms such as bacteria in a sample. A genetically modified bacteriophage is also disclosed which comprises an indicator gene encoding one subunit of an indicator protein. The specificity of the bacteriophage allows detection of a particular bacteria of interest and an indicator signal may be amplified to optimize assay sensitivity.

Assay for real-time simultaneous recruitment of arrestin isoforms (e.g., β-arrestin), to a receptor, such as a G protein-coupled receptor (e.g., DOR); a biosensor; a bioarray; and a kit.

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.