Luciferase Assay Kit                                                                                                                                                                                        Price

Product Description: Luciferase (LUC) encoded by the firefly luciferase gene is widely used as a sensitive reporter enzyme for the study of
transcriptional regulation. The enzyme catalyzes, in the presence of ATP (see ATP Assay Kit), the oxidation of luciferin with concomitant emission
of yellow-green light, which can be conveniently measured by a luminometer or scintillation counter. Light emission peaks in several seconds at
560 nm when the reaction is conducted at pH 7.8 (Anal. Biochem. 80:496,1977). The rapid appearance and decay of the light flash require
consistent timing of the light measurement to obtain reliable data. This provides the basis for an assay system many times more sensitive than the
b-galactosidase (GAL) or other reporter gene systems (PNAS USA 82:7870,1984 & Mol. Cell. Biol. 7:725,1987). The luciferase-based reporter
assay is thus well suited for those cell systems exhibiting low transfection efficiency. The kit is sufficient for 200 assays using 0.1 ml of Luciferase
Substrate per assay. Luciferase Substrate solution if stored in aliquots at -80°C is stable for many years. Repeated freeze-thaw cycles should be
avoided.

Kit Components:

Luciferase Assay Solution: 2 x 10 ml, store at -80°C in small aliquots after the first thawing
10x Cell Lysis Solution: 25 ml, store at 4°C

MSDS: TX-100, Tris, luciferin, EDTA, DTT

Related kits: beta-Galactosidase (LacZ) Assay, beta-Galactosidase (LacZ) Staining, ALP Assay, ATP Assay

Citation:
Lee et al
Influence of promoter potency on the transcriptional effects of YY1, SRF, and Msc-1 in transient transfection analysis
Nucleic Acids Res 26:3215-3220,1998
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The trans-activation activity of the GAL4
fusion protein was tested using a
luciferase reporter construct regulated by
a promoter element driven by
multimerized GAL4 binding sites. The
cotransfection study reveals the
transcriptional activation domain of YY1,
which resides within the N-terminal
138-amino acid region.
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