1.13.12.7: firefly luciferase
This is an abbreviated version!
For detailed information about firefly luciferase, go to the full flat file.
Word Map on EC 1.13.12.7
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1.13.12.7
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bioluminescence
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luminescence
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chemiluminescence
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emit
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renilla
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noninvasive
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luciferases
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cypridina
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photon
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lentiviral
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adenovirus
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click
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luciferase-expressing
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herpes
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engraft
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nude
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co-transfected
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cytomegalovirus
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camera
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electroporation
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simplex
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hsp70
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emitter
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replication-deficient
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excited-state
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promoter-driven
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charge-coupled
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nonviral
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nanoluc
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non-invasively
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gaussia
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luminol
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intramyocardial
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coelenterazine
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bicistronic
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yellow-green
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molecular biology
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light-emitting
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cap-independent
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aequorin
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biotechnology
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red-shifted
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dnaj
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luminometer
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grpe
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polyethylenimine
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bioimaging
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luciferase-based
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medicine
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photoproteins
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glow
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analysis
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multicolor
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brighter
- 1.13.12.7
-
bioluminescence
-
luminescence
-
chemiluminescence
-
emit
- renilla
-
noninvasive
- luciferases
- cypridina
-
photon
-
lentiviral
- adenovirus
-
click
-
luciferase-expressing
-
herpes
-
engraft
-
nude
-
co-transfected
- cytomegalovirus
-
camera
-
electroporation
- simplex
- hsp70
-
emitter
-
replication-deficient
-
excited-state
-
promoter-driven
-
charge-coupled
-
nonviral
- nanoluc
-
non-invasively
- gaussia
- luminol
-
intramyocardial
- coelenterazine
-
bicistronic
-
yellow-green
- molecular biology
-
light-emitting
-
cap-independent
- aequorin
- biotechnology
-
red-shifted
- dnaj
-
luminometer
- grpe
- polyethylenimine
-
bioimaging
-
luciferase-based
- medicine
-
photoproteins
-
glow
- analysis
-
multicolor
-
brighter
Reaction
Synonyms
AL1, AL2, beetle luciferase, CBG99luc, CBRluc, FFL, firefly luciferase, firefly luciferin luciferase, fluc, LpLuc1, LpLuc2, Luc, Luc1, Luc1-type luciferase, Luc2, Luc2-type luciferase, luciferase, luciferase (firefly luciferin), luciferase FM, luciferin, Luciola italica luciferase, lucPpe, lucPpy, orange light-producing luciferase, oxygen 4-oxidoreductase, PC3-Luc, Photinus luciferin 4-monooxygenase (ATP-hydrolyzing), Photinus pyralis luciferase, PML, PpLase, Ppy, Ppy GR-TS, Ppy RE-TS, PpyWT, PsntWT
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1.13.12.7 firefly luciferaseAdvanced search results
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Application on EC 1.13.12.7 - firefly luciferase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biotechnology
industry
the enzyme is widely used in academia and industry due to its excellent sensitivity and dynamic range, and its ease of use
medicine
molecular biology
additional information
analysis
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luminescence-based assays for ATP measurement in clinical chemistry and hygiene monitoring
analysis
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development of a quantitative and highly sensitive luciferase-based assay for bacterial toxins, overview
analysis
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expression of bioluminescent luciferase can be used for rapid and high throughput screening of drugs, e.g. quinolines, acting on Leishmania amastigote-harbouring macrophages and for quantitative real-time monitoring of parasitism features in living mice, overview
analysis
analytical assay of metabolites like ATP, CoA, pyrophosphate, AMP
analysis
Cypridina noctiluca luciferase is utilized for biochemical and molecular biological applications, including bioluminescent enzyme immunoassays, far-red luminescence imaging, and high-throughput reporter assays
analysis
the secreted Cypridina luciferase (CLuc) is used as an ex vivo indicator to continuously monitor tumor progression. On the other hand, the non-secreted firefly luciferase is used as an in vivo indicator to analyze the spatial distribution of the tumor at suitable time points indicated by CLuc. Tumor monitoring systems using dual luciferases are available, allowing long-term bioluminescence imaging under minimal stress for the experimental animals, e.g. BALB/cAJcl-nu/nu mice
analysis
an engineered, commercial thermostable luciferase is suitable for real-time monitoring of ATP release by bacteria, both in broth culture and on agar surfaces, which allows for the estimation of viable cell number by relating luminescence onset time to initial cell concentration. The method is able to rapidly detect the effect of antibiotics on bacterial cultures
analysis
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luciferase-based determination of ATP/NAD(H) pools in combination with a microplate reader and the marine model bacterium Phaeobacter inhibens. Grey multiwell plates best balance sensitivity and crosstalk, and optimal incubation times are 5 min and 30 min for the ATP and NAD(H) assay, respectively, together allowing limits of detection of 0.042, 0.470 and 0.710 nM for ATP, NAD+, and NADH, respectively
analysis
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luciferase-based determination of ATP/NAD(H) pools in combination with a microplate reader and the marine model bacterium Phaeobacter inhibens. Grey multiwell plates best balance sensitivity and crosstalk, and optimal incubation times are 5 min and 30 min for the ATP and NAD(H) assay, respectively, together allowing limits of detection of 0.042, 0.470 and 0.710 nM for ATP, NAD+, and NADH, respectively
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biotechnology
molecular biology studies with luciferase as reproter gene, bioimaging
biotechnology
extensive and advantageous application of this enzyme in biotechnology is restricted due to its low thermal stability
medicine
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luciferase gene is a useful reporter gene in vivo, allowing noninvasive imaging of tumor growth, metastasis, gene transfer, drug treatment, and gene expression. The use of thermostabilized luciferases may allow monitoring of micro-metastses and the early stages of tumor growth
molecular biology
Cypridina noctiluca luciferase is utilized for biochemical and molecular biological applications, including bioluminescent enzyme immunoassays, far-red luminescence imaging, and high-throughput reporter assays
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
molecular biology
Ppy luciferase can been used extensively as a reporter gene in living cells and organisms. Some biological applications are limited by the low stability of the luciferase and limited intracellular luciferin concentration. The mutant enzyme T214A/A215L/I232A/F295L/E345K/I423L/D436G/L530R exhibits both improved thermostability and brighter luminescence at low luciferin concentrations, it may be useful for reporter gene applications
molecular biology
the enzyme is a powerful tool for molecular and cellular biology, and popular in high-throughput screening and drug discovery
additional information
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the combined mutant luciferase, which has high luminescence intensity, will be useful for detecting bacteria with high sensitivity in production safety tests
additional information
the combined mutant luciferase, which has high luminescence intensity, will be useful for detecting bacteria with high sensitivity in production safety tests
