10476498001
Roche
Luciferase
from Photobacterium fischeri
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About This Item
Produits recommandés
Source biologique
bacterial (Photobacterium fischeri)
Conditionnement
pkg of 2 mg
Fabricant/nom de marque
Roche
pH optimal
6.8
Conditions d'expédition
wet ice
Description générale
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.
Application
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
Actions biochimiques/physiologiques
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.
Qualité
Contaminants: <10 mU NADH:FMN oxidoreductase/mg protein, <10 mU myokinase/mg protein, and <1 mU NADH oxidase/mg protein
Stockage et stabilité
Store at 2 to 8 °C. (A decrease in activity of approximately 20% may occur within 12 months.)
Autres remarques
For life science research only. Not for use in diagnostic procedures.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
No data available
Point d'éclair (°C)
No data available
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Les clients ont également consulté
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
Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate.
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
Articles
Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.
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