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Merck

L8507

Sigma-Aldrich

Luciferase from Vibrio fischeri (Photobacterium f)

lyophilized powder

Sinónimos:

Bacterial Luciferase, Luciferase from Photobacterium fischeri

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

composition

Protein, ~40% biuret

storage temp.

−20°C

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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

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

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Los clientes también vieron

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
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
Thomas E Crowley
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 39(2), 126-132 (2011-03-30)
The genes responsible for luminescence in various species of the marine microorganism Photobacterium, have been used for many years as a tool by researchers and instructors. In particular, the lux operon of Photobacterium fischeri has been used by many instructors
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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