L8507
Luciferase from Vibrio fischeri (Photobacterium f)
lyophilized powder
Synonym(s):
Bacterial Luciferase, Luciferase from Photobacterium fischeri
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About This Item
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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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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.
Biochemistry, 48(26), 6085-6094 (2009-05-14)
Bacterial luciferase from Vibrio harveyi is a heterodimer composed of a catalytic alpha subunit and a homologous but noncatalytic beta subunit. Despite decades of enzymological investigation, structural evidence defining the active center has been elusive. We report here the crystal
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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