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L8507

Sigma-Aldrich

Luciferase from Vibrio fischeri (Photobacterium f)

lyophilized powder

Synonyme(s) :

Bacterial Luciferase, Luciferase from Photobacterium fischeri

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Niveau de qualité

Composition

Protein, ~40% biuret

Température de stockage

−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.

Caractéristiques et avantages

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.

Autres remarques

ATCC No. 7744 balance primarily buffer salts and stabilizer.

Forme physique

Partially purified lyophilized powder

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Les clients ont également consulté

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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
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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

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