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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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
Nina E Virolainen et al.
Journal of agricultural and food chemistry, 56(23), 11065-11070 (2008-11-13)
Tetracycline (TC) specific luminescent bacterial biosensors were used in a rapid TC residue assay sensitized to meet the EU maximum residue limit (MRL) for TC residues in poultry muscle tissue (100 microg kg(-1)) by membrane-permeabilizing and chelating agents polymyxin B
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
Prashant K Sharma et al.
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Loredana Peca et al.
FEMS microbiology letters, 289(2), 258-264 (2008-11-20)
Two whole-cell bioluminescent reporters were constructed by fusing the reporter genes luxAB with the Co(2+) and Zn(2+) inducible coaT promoter or the Ni(2+)-inducible nrsBACD promoter, respectively, in the genome of Synechocystis sp. PCC 6803. The obtained reporters, designated coaLux and
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