LUCIFERASE Chemical Properties

Flash point:

111℃

storage temp. 

-20°C

form 

powder

color 

white

Specific Activity

15-30×106light units/mg protein

Safety Information

Hazard Codes 

Xi,Xn,T

Risk Statements 

36/37/38-22-52/53-45

Safety Statements 

26-36/37-24/25-23-22-61-45-53

WGK Germany 

3

F 

3-10-21

MSDS

• Language:English Provider:SigmaAldrich

LUCIFERASE Usage And Synthesis

Description

Luciferase (firefly recombinant) is a light-generating enzyme that catalyzes an oxidative reaction, using luciferin, ATP, and molecular oxygen to produce oxyluciferin, which yields visible light. The bioluminescence of this ATP-dependent luciferase is commonly used in reporter systems that are amenable to high-throughput screening.

Uses

Firefly luciferase is used extensively in molecular and cell biology, in particular for the efficient detection and quantitation of ATP and as a reporter for genetic function.

Uses

Luciferase from Photinus pyralis (firefly) has been used as a component of lysis solution to measure luminescence signals, as part of the study to determine chemical signals which can activate the karrikin insensitive 2 (KAI2) pathway.

General Description

Firefly luciferase catalyzes the reaction of luciferin with ATP and leads to the production of yellow-green light. The enzyme has a molecular weight of 62kDa and is expressed in peroxisomes. Luciferase is considered as a model to study protein–anesthetic interactions. Firefly luciferase is highly useful in cell biology and molecular biology, as a reporter of gene function and for the quantification of ATP.

Biochem/physiol Actions

Firefly luciferase is a 62 kDa protein that catalyzes the production of light. The enzyme requires ATP, molecular oxygen, and the heterocyclic compound, firefly luciferin, to generate light in a two-step process. The light producing reaction is initiated by luciferin activation (adenylation of its carboxylate group) and proceeds in the presence of molecular oxygen to yield a photon of yellow-green light.

Description

Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-550 a.a.) and having a molecular mass of 62.9kDa.
Luciferase is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli

Background

Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.

References

[1] BALDWIN T O. Firefly luciferase: the structure is known, but the mystery remains.[J]. Structure, 1996, 4 3: 223-228. DOI: 10.1016/s0969-2126(96)00026-3
[2] TINGTING XU. The Expanding Toolbox of In Vivo Bioluminescent Imaging.[J]. Frontiers in Oncology, 2016: 150. DOI: 10.3389/fonc.2016.00150
[3] De Souza, F.I., Zumiotti, A.V., and Da Silva, C.F. Neuregulins 1-α and 1-β on the regeneration the peripheral nerves[J]. Acta Ortop Bras.

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