10476498001
Roche
Luciferase
from Photobacterium fischeri
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Prodotti consigliati
Origine biologica
bacterial (Photobacterium fischeri)
Confezionamento
pkg of 2 mg
Produttore/marchio commerciale
Roche
pH ottimale
6.8
Condizioni di spedizione
wet ice
Descrizione generale
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.
Applicazioni
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
Azioni biochim/fisiol
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.
Qualità
Contaminants: <10 mU NADH:FMN oxidoreductase/mg protein, <10 mU myokinase/mg protein, and <1 mU NADH oxidase/mg protein
Stoccaggio e stabilità
Store at 2 to 8 °C. (A decrease in activity of approximately 20% may occur within 12 months.)
Altre note
For life science research only. Not for use in diagnostic procedures.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
No data available
Punto d’infiammabilità (°C)
No data available
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I clienti hanno visto anche
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
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
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
Interspecific luciferase beta subunit hybrids between Vibrio harveyi, Vibrio fischeri and Photobacterium leiognathi
Almashanu S, et al.
Protein engineering, design & selection : PEDS, 9(9), 803-809 (1996)
Articoli
Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.
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