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Documentos Principais

10476498001

Roche

Luciferase

from Photobacterium fischeri

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About This Item

Número da licença da enzima:
Código UNSPSC:
12352204

fonte biológica

bacterial (Photobacterium fischeri)

embalagem

pkg of 2 mg

fabricante/nome comercial

Roche

pH ideal

6.8

Condições de expedição

wet ice

Descrição geral

Contents: Lyophilizate
Specific activity: Approximately 15 mU/mg protein at +25°C with FMN and myristine aldehyde as the substrates, and 50 mU NAD(P)H:FMN oxidoreductase per ml assay solution (based on the relative light emission in the ATP system under the formation of pyrophosphate with 1 mU luciferase from Photinus pyralis).
Alkanal reduced FMN-oxygen oxidoreductase (1-hydroxylating, luminescing)
Luciferase from bacteria exists as a heterodimer with α and β chains.

Aplicação

Luciferase may be used:
  • to treat mammary tumor cryosections for bioluminescence imaging studies
  • as a component of luciferase reaction mixture
  • in bioluminescence assay membrane preparations of Zymomonas mobilis

Ações bioquímicas/fisiológicas

Luciferase catalyzes the conversion of reduced flavin mononucleotide in the presence of oxygen and long-chain aldehyde to flavin mononucleotide, visible light and a fatty acid. It is a reporter enzyme for sensitive quantitation. The lucifearse fusion proteins have been useful in many protein based interaction studies especially in living cells.

Qualidade

Contaminants: <10 mU NADH:FMN oxidoreductase/mg protein, <10 mU myokinase/mg protein, and <1 mU NADH oxidase/mg protein

Armazenamento e estabilidade

Store at 2 to 8 °C. (A decrease in activity of approximately 20% may occur within 12 months.)

Outras notas

For life science research only. Not for use in diagnostic procedures.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

No data available

Ponto de fulgor (°C)

No data available


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A Eberhard et al.
Biochemistry, 20(9), 2444-2449 (1981-04-28)
Synthesis of bacterial luciferase in some strains of luminous bacteria requires a threshold concentration of an autoinducer synthesized by the bacteria and excreted into the medium. Autoinducer excreted by Photobacterium fischeri strain MJ-1 was isolated from the cell-free medium by
S Walenta et al.
International journal of radiation oncology, biology, physics, 51(3), 840-848 (2001-11-09)
It has been shown that oxygen gradients exist in R3230AC tumors grown in window chambers. The fascial surface is better oxygenated than the tumor surface. The purpose of the present study was to determine whether gradients exist for energy metabolites
Nicole Feldmann et al.
Molecular and cellular endocrinology, 338(1-2), 46-57 (2011-03-05)
Glutamate is generated during nutrient stimulation of pancreatic islets and has been proposed to act both as an intra- and extra-cellular messenger molecule. We demonstrate that glutamate is not co-secreted with the hormones from intact islets or purified α- and
Mary P Hall et al.
ACS chemical biology, 7(11), 1848-1857 (2012-08-17)
Bioluminescence methodologies have been extraordinarily useful due to their high sensitivity, broad dynamic range, and operational simplicity. These capabilities have been realized largely through incremental adaptations of native enzymes and substrates, originating from luminous organisms of diverse evolutionary lineages. We
Uldis Kalnenieks et al.
Microbiology (Reading, England), 149(Pt 7), 1739-1744 (2003-07-12)
The respiratory inhibitor cyanide stimulates growth of the ethanologenic bacterium Zymomonas mobilis, perhaps by diverting reducing equivalents from respiration to ethanol synthesis, thereby minimizing accumulation of toxic acetaldehyde. This study sought to identify cyanide-sensitive components of respiration. In aerobically grown

Artigos

Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.

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