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from Photobacterium phosphoreum * Pricing updated September 23rd, 2011. Prices are subject to change without notice. Shipping charges are not included. For other size, please contact us Click to order or to get further information |
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Synonyms: Alkanal, reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing)
NOVOCIB's bacterial luciferase is purified from a Photobacterium phosphoreum strain isolated from squid by our team and selected for its brightest luminescence. The luxab gene was amplified by PCR and cloned. The sequences of cloned α and β subunits have shown 94% and 92% identity to P24113 and P12744 proteins of Photobacterium phosphoreum (SwissProt Entry).
Applications: In luminescent marine photobacteria, the production of light results from two successive reactions.
The first one is catalyzed by the NAD(P)H-FMN oxidoreductase (EC 1.6.8.1), that produces FMNH2 acting as a substrate for the second reaction, which is catalyzed by a luciferase (EC 1.14.14.3) to generate light in the presence of an aliphatic aldehyde and molecular oxygen.
In the presence of limiting concentrations of NADH substrate, light intensity is proportional to NAD(P)H concentration. The coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for the quantification of NAD(P)H and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol, oxaloacetate)(1).
NOVOCIB's Highly Pure Bacterial Luciferase can be used for NAD(P)H quantification or in dehydrogenase-coupled assays.
The enzyme is provided lyophilized, alone or with lyophilized FMN-reductase (Ref. #E-Nov 8).
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Applications: In luminescent marine photobacteria, the production of light results from two successive reactions.
The first one is catalyzed by the NAD(P)H-FMN oxidoreductase (EC 1.6.8.1), that produces FMNH2 acting as a substrate for the second reaction, which is catalyzed by a luciferase (EC 1.14.14.3) to generate light in the presence of an aliphatic aldehyde and molecular oxygen.
In the presence of limiting concentrations of NADH substrate, light intensity is proportional to NAD(P)H concentration. The coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for the quantification of NAD(P)H and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol, oxaloacetate)(1).
NOVOCIB's Highly Pure Bacterial Luciferase can be used for NAD(P)H quantification or in dehydrogenase-coupled assays.
The enzyme is provided lyophilized, alone or with lyophilized FMN-reductase (Ref. #E-Nov 8).
 Purity: controlled by 10% AA SDS-PAGE. |
Figure 1: Calibration curves (log-log plot) for NADH obtained using Highly Pure Bacterial Luciferase (50µg/ml, NovoCIB, E-Nov 10).
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