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AB100961

Recombinant Firefly Luciferase protein

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(4 Publications)

Recombinant Firefly Luciferase protein is a Firefly Full Length protein, in the 1 to 550 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE and mass spectrometry.The predicted molecular weight of ab100961 protein is 63 kDa.

- Save time and ensure accurate results - use our recombinant Firefly Luciferase as a control
- Available in different sizes to fit your experimental needs

View Alternative Names

Luciferin 4-monooxygenase, Luciferase

1 Images
SDS-PAGE - Recombinant Firefly Luciferase protein (AB100961)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Firefly Luciferase protein (AB100961)

15% SDS-PAGE showing ab100691 (3 μg) at approximately 62.9 kDa.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P08659

Animal free

No

Carrier free

No

Species

Firefly

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Ensure the validity of your result using our recombinant Firefly Luciferase protein ab100961 as a control in SDS-PAGE and mass spectrometry.


Check out our protein gel staining guide for SDS-PAGE here
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMMEDAKNIKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIKAKKGGKIAV","proteinLength":"Full Length","predictedMolecularWeight":"62.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":550,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P08659","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Firefly luciferase also known as luc assay or luciferase protein is an enzyme that catalyzes the oxidation of luciferin resulting in bioluminescence. This protein has a molecular mass of approximately 61 kDa and is responsible for the characteristic glow of fireflies. The luciferase expression occurs mainly in the light-producing organs of fireflies such as in the insect Photinus pyralis where it plays an important role in light emission.
Biological function summary

Firefly luciferase converts chemical energy into light making it valuable for various biological applications as a reporter gene. It participates in the formation of a complex with its substrates luciferin and ATP resulting in the production of a photon. This enzyme is widely used in molecular and cellular biology experiments to monitor gene expression and study protein-protein interactions due to its luminescent properties.

Pathways

Firefly luciferase functions in the bioluminescent pathway involving the conversion of luciferin to oxyluciferin and light emission. It interfaces with ATP a universal energy carrier which highlights its integration into the cellular energy systems. Firefly luciferase is similar to other oxidative enzymes though it is not directly involved with metabolic pathways like the TCA cycle or glycolysis.

Researchers often utilize firefly luciferase as a tool in tumor studies or infectious disease models. Its luminescence aids in imaging and tracking biological processes in real-time. While firefly luciferase itself is not directly associated with specific diseases the use of firefly agents allows researchers to study disease outcomes assess therapeutic efficacy and understand gene expression profiles related to cancer and viral infections often in connection with proteins such as p53 in cancer research.
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Specifications

Form

Liquid

Additional notes

ab100961 is purified using conventional chromatography techniques.

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General info

Function

Produces green light with a wavelength of 562 nm.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Subcellular localisation

Peroxisome

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Product protocols

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Target data

Produces green light with a wavelength of 562 nm.
See full target information Luciferin 4-monooxygenase
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Publications (4)

Recent publications for all applications. Explore the full list and refine your search

BMC cancer 22:844 PubMed35922758

2022

Characterization and comparison of human glioblastoma models.

Applications

Unspecified application

Species

Unspecified reactive species

Julia A Schulz,Louis T Rodgers,Richard J Kryscio,Anika M S Hartz,Björn Bauer

Biotechnology and bioengineering 118:186-198 PubMed32910455

2020

Knockout of the caspase 8-associated protein 2 gene improves recombinant protein expression in HEK293 cells through up-regulation of the cyclin-dependent kinase inhibitor 2A gene.

Applications

Unspecified application

Species

Unspecified reactive species

Laura Abaandou,Ashish K Sharma,Joseph Shiloach

Nature communications 10:76 PubMed30622267

2019

Thrombospondin-3 augments injury-induced cardiomyopathy by intracellular integrin inhibition and sarcolemmal instability.

Applications

Unspecified application

Species

Unspecified reactive species

Tobias G Schips,Davy Vanhoutte,Alexander Vo,Robert N Correll,Matthew J Brody,Hadi Khalil,Jason Karch,Andoria Tjondrokoesoemo,Michelle A Sargent,Marjorie Maillet,Robert S Ross,Jeffery D Molkentin

Medical sciences (Basel, Switzerland) 6: PubMed29890687

2018

Knocking out Ornithine Decarboxylase Antizyme 1 () Improves Recombinant Protein Expression in the HEK293 Cell Line.

Applications

Unspecified application

Species

Unspecified reactive species

Laura Abaandou,Joseph Shiloach
View all publications
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