L8507
Luciferase from Vibrio fischeri (Photobacterium f)
lyophilized powder
Synonym(s):
Bacterial Luciferase, Luciferase from Photobacterium fischeri
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-751-7
MDL number:
Product Name
Luciferase from Vibrio fischeri (Photobacterium f), lyophilized powder
form
lyophilized powder
composition
Protein, ~40% biuret
storage temp.
−20°C
Quality Level
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Application
Luciferase from Vibrio fischeri has been used in a study to assess kinetics of light emission and oxygen consumption by bioluminescent bacteria. It has also been used in a study to investigate the sensitivity of dark mutants of various strains of luminescent bacteria to reactive oxygen species.
Features and Benefits
Partially purified, soluble extracts containing FMN-dependent luciferase and NADH- and NADPH-dependent FMN reductases. Produces light in a system containing FMN, NADH or NADPH, and n-decyl aldehyde.
Other Notes
ATCC No. 7744 balance primarily buffer salts and stabilizer.
Physical form
Partially purified lyophilized powder
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Patricia G Cruz et al.
Chemistry & biology, 18(11), 1442-1452 (2011-11-29)
The chemical diversity of nature has tremendous potential for the discovery of molecular probes and medicinal agents. However, sensitivity of HTS assays to interfering components of crude extracts derived from plants, and macro- and microorganisms has curtailed their use in
J J Bourgois et al.
Journal of bioenergetics and biomembranes, 33(4), 353-363 (2001-11-17)
Oxygen plays a key role in bacterial bioluminescence. The simultaneous and continuous kinetics of oxygen consumption and light emission during a complete exhaustion of the exogenous oxygen present in a closed system has been investigated. The kinetics are performed with
Zachary T Campbell et al.
The Journal of biological chemistry, 284(13), 8322-8328 (2009-01-14)
Unlike the vast majority of flavoenzymes, bacterial luciferase requires an exogenous source of reduced flavin mononucleotide for bioluminescence activity. Within bioluminescent bacterial cells, species-specific oxidoreductases are believed to provide reduced flavin for luciferase activity. The source of reduced flavin in
Zachary T Campbell et al.
Biophysical journal, 99(12), 4012-4019 (2010-12-16)
Bacterial luciferase contains an extended 29-residue mobile loop. Movements of this loop are governed by binding of either flavin mononucleotide (FMNH2) or polyvalent anions. To understand this process, loop dynamics were investigated using replica-exchange molecular dynamics that yielded conformational ensembles
Cexia Mei et al.
Wei sheng wu xue bao = Acta microbiologica Sinica, 49(9), 1223-1228 (2009-12-25)
The study aimed at establishing the bacterial luciferase: FMN-NADH oxidoreductase bioluminescent system in vitro and evaluating its potential for quantitative detection of NADH. By optimizing the amount of substrates, we set up the coupled luciferase: FMN-NADH oxidoreductase bioluminescent system in
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