GFP isolated from jellyfish Aequorea Victoria exhibited spontaneous fluorescence property. It is a novel important marker for gene expression in various heterologous systems. It is stably present in plant cells and shows photobleaching. Molecular cloning of GFP produces a fused protein with fluorescence excitation and emission spectra.
Heat inactivation: Fluorescence will be quenched by reducing reagents, such as DTT or sodiumdithiosulfate, and is completely inhibited by peroxide.
Fluorescence is inhibited by extreme pH conditions (pH < 4 and pH > 11) as well as ethanol content higher than 60%.
Recombinant green fluorescent protein (rGFP) has also been used in indirect enzyme-linked immunosorbent assay.
Recombinant Green Fluorescent Protein (rGFP) is suitable as:
- Positive control when detecting GFP fusion proteins by SDS-PAGE.
- Positive control when detecting GFP fusion proteins by western blot using Anti-GFP monoclonal antibody.
- Standard for experiments involving fluorescence microscopy.
Solution, 1 mg/ml rGFP in 5 mM Tris-HCl, 5 mM EDTA, pH 8.0
Working concentration: Amount of rGFP recommended for:
- SDS-PAGE (Coomassie stained): 1 μg
- Western blot: 5 ng
Emission max: 509nm
Excitation max: 395nm
For life science research only. Not for use in diagnostic procedures.