Bacterial Luciferase

Highly Pure Bacterial Luciferase (E.C.1.14.14.3)

Ultra‑pure FMNH₂‑dependent luciferase producing intense bioluminescence for NAD(P)H quantification, enzymatic assays, and high‑sensitivity analytical applications.

from Photobacterium phosphoreum

Derived from a squid‑associated P. phosphoreum strain selected for its brightest luminescence. According to the product sheet, “the luxAB gene was amplified by PCR and cloned, and the α and β subunits show 94% and 92% identity to SwissProt entries P24113 and P12744”.

Ref. #E-Nov10

#REF	Quantity	Price
#E-Nov10-1	1 mg	€ 295.00	Inquiry
#E-Nov10-2	2 mg	€ 488.00	Inquiry
#E-Nov10-5	5 mg	€ 1106.00	Inquiry

Kit is provided in stable lyophilized form & shipped without dry ice.

Bulk quantity available.

Request a quotation at contact@novocib.com

Download NOVOCIB's Bacterial Luciferase

Description

NOVOCIB’s bacterial luciferase is purified from a naturally luminescent Photobacterium phosphoreum strain isolated from squid. The PDF states: “the strain was selected for its brightest luminescence,” and the cloned α and β subunits show high identity to native proteins (94% and 92%).

Mechanism of Bioluminescence

In marine photobacteria, light production results from two sequential enzymatic reactions:

NAD(P)H–FMN oxidoreductase (EC 1.6.8.1) reduces FMN to FMNH₂.
Bacterial luciferase (EC 1.14.14.3) oxidizes FMNH₂ in the presence of an aliphatic aldehyde and oxygen, producing visible light.

The PDF explains: “In the presence of limiting concentrations of NADH, light intensity is proportional to NAD(P)H concentration,” enabling highly sensitive quantification.

Applications

Coupling luciferase with FMN‑NAD(P)H oxidoreductase provides an ultrasensitive system for:

NADH and NADPH quantification
Dehydrogenase‑coupled assays
Measurement of substrates of NADH‑dependent enzymes: glucose, lactate, malate, ethanol, sorbitol, oxaloacetate
Bioluminescent biosensors
Analytical biochemistry and metabolic studies

Activity & Performance

According to the product sheet, the enzyme exhibits:

“>500,000 RLU per second per µg of protein in the presence of 10 µM NADH and 3.5 mU/mL FMN‑reductase”.

Lux gel photo — SDS‑PAGE showing α (39 kDa) and β (36 kDa) subunits.

Lux Calibration Graph — Calibration curve for NADH using 50 µg/mL luciferase. The PDF describes the assay conditions: “0.1 M KH₂PO₄ pH 6.9, 0.02% dodecanal, 50 µM FMN, 2 mg/mL BSA; 15‑second luminescence measurement.”