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L8507

Sigma-Aldrich

Luciferase from Vibrio fischeri (Photobacterium f)

lyophilized powder

Synonym(s):

Bacterial Luciferase, Luciferase from Photobacterium fischeri

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100 MG
$485.00
500 MG
$1,344.00

$485.00

Available to ship onApril 11, 2025Details

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100 MG
$485.00
500 MG
$1,344.00

About This Item

CAS Number:
9014-00-0
Enzyme Commission number:
1.14.14.3 (BRENDA, IUBMB)
EC Number:
232-751-7
MDL number:
MFCD00131545
UNSPSC Code:
12352204
NACRES:
NA.54

$485.00

Available to ship onApril 11, 2025Details

form

lyophilized powder

Quality Level

200

composition

Protein, ~40% biuret

storage temp.

−20°C

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Application

Luciferase from Vibrio fischeri has been used in a study to assess kinetics of light emission and oxygen consumption by bioluminescent bacteria. [1] It has also been used in a study to investigate the sensitivity of dark mutants of various strains of luminescent bacteria to reactive oxygen species. [2]

Features and Benefits

Partially purified, soluble extracts containing FMN-dependent luciferase and NADH- and NADPH-dependent FMN reductases. Produces light in a system containing FMN, NADH or NADPH, and n-decyl aldehyde.

Other Notes

ATCC No. 7744 balance primarily buffer salts and stabilizer.

Physical form

Partially purified lyophilized powder

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000365351
0000311581
0000297670
0000311581
0000365351

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Patricia G Cruz et al.
Chemistry & biology, 18(11), 1442-1452 (2011-11-29)
The chemical diversity of nature has tremendous potential for the discovery of molecular probes and medicinal agents. However, sensitivity of HTS assays to interfering components of crude extracts derived from plants, and macro- and microorganisms has curtailed their use in
J J Bourgois et al.
Journal of bioenergetics and biomembranes, 33(4), 353-363 (2001-11-17)
Oxygen plays a key role in bacterial bioluminescence. The simultaneous and continuous kinetics of oxygen consumption and light emission during a complete exhaustion of the exogenous oxygen present in a closed system has been investigated. The kinetics are performed with
Zachary T Campbell et al.
The Journal of biological chemistry, 284(13), 8322-8328 (2009-01-14)
Unlike the vast majority of flavoenzymes, bacterial luciferase requires an exogenous source of reduced flavin mononucleotide for bioluminescence activity. Within bioluminescent bacterial cells, species-specific oxidoreductases are believed to provide reduced flavin for luciferase activity. The source of reduced flavin in
Nina E Virolainen et al.
Journal of agricultural and food chemistry, 56(23), 11065-11070 (2008-11-13)
Tetracycline (TC) specific luminescent bacterial biosensors were used in a rapid TC residue assay sensitized to meet the EU maximum residue limit (MRL) for TC residues in poultry muscle tissue (100 microg kg(-1)) by membrane-permeabilizing and chelating agents polymyxin B
Zachary T Campbell et al.
Biochemistry, 48(26), 6085-6094 (2009-05-14)
Bacterial luciferase from Vibrio harveyi is a heterodimer composed of a catalytic alpha subunit and a homologous but noncatalytic beta subunit. Despite decades of enzymological investigation, structural evidence defining the active center has been elusive. We report here the crystal
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