14 results about "Luciferin" patented technology

The present application relates to a method for introducing an exogenous caffeic acid synthesis pathway to improve the light intensity of plants, and introducing TAL genes and P450 genes into plants to obtain a significant up-regulation effect of caffeic acid expression amount. This may be because the introduction of TAL genes and P450 genes promotes the deamination of L-DOPA, increases the accumulation amount of L-DOPA, and further effectively increases the caffeic acid expression amount in plants. Based on this pathway, the synthesis of luciferin in plants is increased to enhance the light intensity of plants.

The present disclosure provides a protein having luciferase activity, comprising the secondary structure arrangement H1-L1-H2-L2-B1-L3-B2-L4-H3-L5-B3-L6-B4-L7-B5-L8-B6, wherein (i) “H” is a helical domain, “L” is a loop domain, and “B” is a beta strand domain, wherein the B5 domain is at least 11, 12, 13, or 14 amino acids in length and residue 11 of the B5 domain is F, Y, or L; and the B4 domain is at least 12 amino acids in length and residue 10 of the B4 domain is F, Y, L, I, K or M; and / or residue 12 of the B4 domain is F, L, R, D, M, Q or V; (ii) the H1 domain is at least 18 or 19 amino acids in length; residue 9 of the H1 domain is T, S, H, R, C, L, D, V, A, Q, G, E, K, I, N or M; (iii) the B3 domain is at least 6, 7, 8, 9, or 10 amino acids in length and residue 1 of the B3 domain is W or H; (iv) the B4 domain is at least 12 amino acids in length and residue 10 of the B4 domain is F, Y, L, I, K or M; or (v) the B4 domain is at least 12 amino acids in length and residue 12 of the B4 domain is L, R, D, M, Q or V. Additional proteins disclosed herein are exemplified in the claims. Also provided herein are luciferase substrates, assay buffers, and kits comprising one or more of a protein having luciferase activity or a nucleic acid encoding the protein, an assay buffer, and a luciferase substrate.

In one embodiment, the present application provides a liquid circulating luminescent reagent excellent in stability. In one embodiment, the present application provides a liquid composition for measuring ATP, and AMP and / or ADP in a sample after storage, (i) the liquid composition comprising luciferase, luciferin, an enzyme catalyzing a reaction of generating ATP from AMP, a substrate and a co-factor of the enzyme catalyzing the reaction of generating ATP from AMP, or in the case where at least one of these components is not contained in the liquid composition, the component not contained in the liquid composition is added to the liquid composition before or at the time of measurement, and, (ii) the relative luminescence amount of the liquid composition at the time of storage is 5500 RLU or less, the relative luminescence amount being a value after subtracting a control value from a measurement value.

The present disclosure provides a protein having luciferase activity comprising a secondary structural arrangement H1-L1-H2-L2-B1-L3-B2-L4-H3-L5-B3-L6-L4-L7-L5-L8-B6 wherein (i) "H" is a helical domain, "L" is a loop domain, and "B" is a beta chain domain wherein the length of the B5 domain is at least 11, 12, 13, or 14 amino acids, and wherein "L" is a cyclic domain, and "B" is a beta chain domain. And residue 11 of the B5 domain is F, Y or L; and the length of the B4 domain is at least 12 amino acids, and the residue 10 of the B4 domain is F, Y, L, I, K or M; and / or residue 12 of the B4 domain is F, L, R, D, M, Q or V; (ii) the H1 domain is at least 18 or 19 amino acids in length; the residue 9 of the H1 domain is T, S, H, R, C, L, D, V, A, Q, G, E, K, I, N or M; (iii) the length of the B3 domain is at least 6, 7, 8, 9 or 10 amino acids, and the residue 1 of the B3 domain is W or H; (iv) the length of the B4 domain is at least 12 amino acids, and the residue 10 of the B4 domain is F, Y, L, I, K or M; or (v) the length of the B4 domain is at least 12 amino acids, and the residue 12 of the B4 domain is L, R, D, M, Q, or V. Additional proteins disclosed herein are illustrated in the claims. Also provided herein are luciferase substrates, assay buffers, and kits comprising one or more of a protein having luciferase activity or a nucleic acid encoding the protein, an assay buffer, and a luciferase substrate.

The application relates to the technical field of mobile self-organizing network and flight ad hoc network communication, and discloses an AODV routing method based on Hello message statistical characteristic mapping luciferin. The strategy aims at the problem that the traditional AODV protocol is prone to misjudging the communication gray area as an effective link in a high dynamic network, the Hello message timestamp is extended to perceive link jitter, and multi-dimensional features such as a successful receiving rate and signal strength are combined to carry out normalization processing, so as to construct an instantaneous fitness function; a bionic glowworm swarm optimization mechanism is further introduced to dynamically update luciferin values with historical memory; finally, pruning is implemented according to the luciferin threshold value in the routing discovery stage, so that unstable links are blocked.

Disclosed are ATP-independent bioluminescent reporter systems for enhanced in vivo imaging. Also disclosed is a modified luciferin, potassiorin, comprising a potassium-binding moiety. Also disclosed is an engineered luciferase, BRIPO, optimized for synergistic interaction with potassiorin. A further version of the disclosed system produces bioluminescence signals responsive to physiological potassium concentrations. In further instances, the system enables real-time monitoring of K+ dynamics in live cells, tissues, and animals. A further embodiment includes applications in imaging neuronal activity, studying ion flux, and developing bioluminescent indicators for diverse analytes. The disclosed system addresses limitations of traditional imaging methods, offering improved sensitivity and biocompatibility.

The polypeptide membrane anchoring high-throughput screening method for GPCR is that the C terminal of GPCR is connected with tetracycline-controlled transcriptional activator (tTA) through tobacco etch virus protease substrate sequence (TEV-Substrate). When GPCR is combined with the membrane anchoring polypeptide, the TEV protease cuts the substrate to release tTA, activates the expression of luciferase reporter gene (Luc), and the cell expressing luciferase can detect the production amount of oxidized luciferin by using an enzyme label instrument, so that the accurate screening of the targeted polypeptide compound is realized. The screening method provided by the application can quickly screen the polypeptide combined with GPCR, is not limited to the screening of only a certain signal path in the traditional GPCR function detection, and can realize the high-throughput screening of the polypeptide and GPCR target by combining the luciferase reporter gene.

This invention provides a sterility indicator that does not require complex culture procedures like BI or luciferin-luciferase assays like EI, can be supplied stably at low cost, and can accurately measure sterility intensity in a dry state. [Solution] The device comprises a base material and a sensitive member supported on the base material that is sensitive to the sterilizing agent. The sensitive member is made of a material whose constituent is a fluorescent protein, and genetically modified fluorescent silk is used. This genetically modified fluorescent silk emits fluorescence at a predetermined wavelength when irradiated with excitation light of a predetermined wavelength. The fluorescence intensity of the sensitive member changes in proportion to the exposure intensity of the sterilizing agent to the sensitive member.

Provided is a sterilization indicator that does not require complicated culture operations such as BI or luciferin-luciferase assays such as EI, can be stably supplied at low cost, and makes it possible to accurately measure sterilization intensity in a dry state. The sterilization indicator comprises a base material and a sensitive member that is supported by the base material and is sensitive to a sterilizing agent. The sensitive member is a material having a fluorescent protein as a constituent element, and employs genetically modified fluorescent silk. This genetically modified fluorescent silk emits fluorescence having a prescribed wavelength in response to irradiation of excitation light having a prescribed wavelength. The fluorescence intensity of the sensitive member changes in proportion to the exposure intensity of the sterilizing agent with respect to the sensitive member.

An ultrasensitive and long-lasting luminescence cascade can be used for point-of-care detection. A reaction chamber can receive and incubate a volume of a sample and a volume of magnetic tag solution before the combination is washed. Then, a working solution including d-luciferin-6-O-β-d-galactopyranoside (LUGAL), firefly luciferase (Fluc), and a luminescence buffer comprising ATP can be added to the reaction chamber. When the reaction chamber also includes tagged target components including beta galactosidase (GAL) then the GAL supplies luciferin intermediates that catalyze the cleavage of a protecting group from the LUGAL, generating luciferin, and the Fluc catalyzes the oxidation of D-luciferin in a presence of the ATP and O2, yielding oxyluciferin and luminescence. Repeated catalytic cycles increase a measurable signal of the luminescence. An optical sensor can capture an image of the luminescence and the presence of tagged target components can be determined based on an amount of luminescence in the image.

The invention relates to the technical field of bacterial detection, in particular to a bacterial detection method of lytic vibrio parahaemolyticus bacteriophage. The method comprises the following steps: collecting a sample, preparing a sample homogenate, and pre-enriching to obtain an enrichment liquid; mixing the enrichment liquid with a broad-spectrum bacteriophage reagent to form a reaction system, and performing incubation treatment; an ATP releasing agent is added, a luciferase-fluorescein substrate working solution is added, and a bioluminescence value is measured; the bioluminescence value is converted into ATP concentration, and the original viable bacterium concentration in the sample is calculated. According to the method, based on the high-specificity recognition and lysis effects of the lytic bacteriophage on the vibrio parahaemolyticus, a sample and a high-specificity vibrio parahaemolyticus lytic bacteriophage mixture are jointly incubated, and the bacteriophage can efficiently infect and lyse living vibrio parahaemolyticus existing in the sample; and further analyzing the cracking product of the vibrio parahaemolyticus to realize rapid and specific detection of the quantity of the original viable bacteria in the sample.

The present invention concerns bioluminescent plants and methods for producing them. Among said methods, the invention relates, in particular, to a method of introducing luciferase genes and luciferin biosynthesis genes into the chloroplasts of a plant. In addition, the invention concerns a method of producing light comprising adding chemical compounds to a culture medium of the plant according to the invention.

In one embodiment, the objective of the present invention is to provide a liquid cyclic luminescent reagent with excellent stability. In one embodiment, the present invention provides a liquid composition for measuring ATP, AMP and / or ADP in a sample after preservation, (i) the liquid composition comprising luciferase, luciferin, an enzyme catalyzing the reaction from AMP to ATP, a substrate of the enzyme catalyzing the reaction from AMP to ATP, and a cofactor, or, if the liquid composition does not contain at least one of these components, the components not contained in the liquid composition are added to the liquid composition before or during the measurement, and (ii) the relative luminescence intensity of the liquid composition at preservation is 5500 RLU or less, the relative luminescence intensity being the value obtained by subtracting a control value from the measured value.

In one embodiment, an object of the present invention is to provide a liquid cycling luminescent reagent having excellent stability.SOLUTION: In one embodiment, the present invention provides a liquid composition for measuring ATP, and AMP and / or ADP in a sample after storage, comprising (I) luciferase, luciferin, an enzyme that catalyzes a reaction of generating ATP from AMP, a substrate for the enzyme that catalyzes a reaction of generating ATP from AMP, and a cofactor, or when at least one of these components is not contained in the liquid composition, the component not contained in the liquid composition is added to the liquid composition before or during the measurement, (ii) a relative light unit of the liquid composition during storage is equal to or less than 5500RLU, wherein the relative light unit is obtained by subtracting a control value from a measured value.SELECTED DRAWING: Figure 2