Results 241 to 250 of about 11,605 (288)
Some of the next articles are maybe not open access.
Coelenterazine-dependent luciferases
Biochemistry (Moscow), 2015Bioluminescence is a widespread natural phenomenon. Luminous organisms are found among bacteria, fungi, protozoa, coelenterates, worms, molluscs, insects, and fish. Studies on bioluminescent systems of various organisms have revealed an interesting feature - the mechanisms underlying visible light emission are considerably different in representatives ...
S V, Markova, E S, Vysotski
openaire +2 more sources
Introduction to beetle luciferases and their applications
Luminescence, 1989AbstractAll beetle luciferases have evolved from a common ancestor: they all use ATP, O2, and a common luciferin as substrates. The most studied of these luciferases is that derived from the firefly Photinus pyralis, a beetle in the superfamily of Cantharoidea.
Keith V Wood, W D Mcelroy
exaly +3 more sources
Cold Spring Harbor Protocols, 2010
INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
openaire +2 more sources
INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
openaire +2 more sources
Flavin binding by bacterial luciferase: Affinity chromatography of bacterial luciferase
Biochemical and Biophysical Research Communications, 1974Abstract Immobilized FMN covalently attached to Sepharose-6B-hexanoate binds bacterial luciferase. Immobilized flavin is also effective in its reduced form as a substrate in the light emitting reaction catalyzed by luciferase.
C A, Waters, J R, Murphy, J W, Hastings
openaire +2 more sources
2006
Luciferase is the ideal reporter gene to provide temporal and spatial information on promoter activity in Arabidopsis and other eukaryotes; the noninvasive detection of luminescence and short half-life of luciferase activity allow repeated measurements of individual seedlings over several days to assay dynamic changes in gene expression.
Megan M, Southern +2 more
openaire +2 more sources
Luciferase is the ideal reporter gene to provide temporal and spatial information on promoter activity in Arabidopsis and other eukaryotes; the noninvasive detection of luminescence and short half-life of luciferase activity allow repeated measurements of individual seedlings over several days to assay dynamic changes in gene expression.
Megan M, Southern +2 more
openaire +2 more sources
2006
This luciferase reporter assay provides a simple and highly sensitive method to determine the responsiveness of the Tet-system. It is quantitative, reproducible and easy to use in DT40 screens with both transient and stable transfections. The reaction catalyzed by firefly luciferase is the oxidation of luciferin in the presence of coenzyme A with ...
Frank R, Wettey, Antony P, Jackson
openaire +2 more sources
This luciferase reporter assay provides a simple and highly sensitive method to determine the responsiveness of the Tet-system. It is quantitative, reproducible and easy to use in DT40 screens with both transient and stable transfections. The reaction catalyzed by firefly luciferase is the oxidation of luciferin in the presence of coenzyme A with ...
Frank R, Wettey, Antony P, Jackson
openaire +2 more sources
Measurement of Luciferase Rhythms
2014Firefly luciferase (LUC) is a sensitive and versatile reporter for the analysis of gene expression. Transgenic plants carrying CLOCK GENE promoter:LUC fusions can be assayed with high temporal resolution. LUC measurement is sensitive, noninvasive, and nondestructive and can be readily automated, greatly facilitating genetic studies.
C Robertson, McClung, Qiguang, Xie
openaire +2 more sources
Dual Luciferase Assay for Secreted Luciferases Based on Gaussia and NanoLuc
ASSAY and Drug Development Technologies, 2013Just recently, NanoLuc, a new engineered luciferase based on the small subunit of the luciferase from Oplophorus gracilirostris was introduced. Like the luciferase from Gaussia princeps, this luciferase is secreted into the medium. Both luciferases are the smallest and brightest luciferases known and well-suited for reporter assays. In our experiments,
Kerstin, Heise +4 more
openaire +2 more sources
Fabrication of a New Lineage of Artificial Luciferases from Natural Luciferase Pools
ACS Combinatorial Science, 2017The fabrication of artificial luciferases (ALucs) with unique optical properties has a fundamental impact on bioassays and molecular imaging. In this study, we developed a new lineage of ALucs with unique substrate preferences by extracting consensus amino acids from the alignment of 25 copepod luciferase sequences available in natural luciferase pools.
Sung Bae Kim +3 more
openaire +2 more sources
Biotechnology Letters, 2013
NanoLuc luciferase (Nluc) is an engineered enzyme that catalyses the substrate, furimazine, to produce light. Nluc has higher sensitivity than the commonly used bioluminescent reporter, firefly luciferase (FFluc). We have introduced Nluc into a toxin-antitoxin stabilised plasmid for the efficient labeling of group A Streptococcus.
Jacelyn M S, Loh, Thomas, Proft
openaire +2 more sources
NanoLuc luciferase (Nluc) is an engineered enzyme that catalyses the substrate, furimazine, to produce light. Nluc has higher sensitivity than the commonly used bioluminescent reporter, firefly luciferase (FFluc). We have introduced Nluc into a toxin-antitoxin stabilised plasmid for the efficient labeling of group A Streptococcus.
Jacelyn M S, Loh, Thomas, Proft
openaire +2 more sources