| Field | Specification |
|---|---|
| Target | |
| Alternative names | Luciferase; Firefly Luciferase |
| Applications | |
| Tag | |
| Expression system | |
| Expression region | |
| Molecular weight | |
| Protein length | |
| Purity | |
| Biological activity | |
| Formulation | |
| Storage | |
| Shipping | |
| Catalog no. (Mfr.) | |
| Main SKU |
Background
LUCIFERASE is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: Luciferase; Firefly Luciferase.
Firefly Luciferase, Preparation method: E. coli
Firefly Luciferase catalyzes the reaction of luciferin with ATP and results in the production of yellow-green light. The enzyme has a molecular weight of 62 kDa and is expressed in peroxisomes. Luciferase is considered a model forstudying protein-anesthetic interactions. Firefly Luciferase is very useful in cell biology and molecular biology as a reporter of gene function and for the quantification of ATP
Biological significance and function
LUCIFERASE is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as Molecular & Cellular Biology.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Molecular weight: 62 kDa
- Protein length: The recombinant Firefly Luciferase predicts a molecular mass of 62 kDa.
- Expression region: Amino acid sequence of luciferase derived from Photinus pyralis (firefly)was expressed with 6×His tag at the N-terminus.
- Purity: > 98 % as determined by SDS-PAGE
- Biological activity: >109 RLU/mg protein as determined in the presence of ATP and luciferin.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: His tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: Liquid in from sterile 20 mM Tris, 150 mM NaCl, 1mM DTT, pH 8.0. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.
