EC Number |
Application |
Reference |
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1.13.12.5 | analysis |
an advanced Fc-binding probe, FcUni-RLuc, is produced and functionally assayed for labelling IgGs. The Fc antibody binding sequence HWRGWV is fused to Renilla luciferase, and the purified probe is employed for bioluminescence enzyme-linked immunoabsorbance assay of Her2 positive cells |
744017 |
1.13.12.5 | analysis |
analysis of luciferase inhibitors by quantitative high-throughput screening and comparison of and structure-activity relationship using various luciferase-based detection reagents |
688275 |
1.13.12.5 | analysis |
development of a bioluminiscent probe composed of peptide EYFP and luciferase for near-real-time single-cell imaging using bioluminescence resonance energy transfer BRET. The probe exhibits enhanced luciferase luminescence intensity and appropriate subcellular distribution when it is fused to targeting-signal peptides or histone H2AX. It allows high spatial and temporal resolution microscopy of living cells |
689133 |
1.13.12.5 | analysis |
enhanced-sensitivity, synthetically facile reporter fusion to merge the bioluminescence output of Gaussia luciferase with the biotin-binding ability of tamavidin 2. The fusion construct enables direct bacterial expression of a reporter system incorporating two functionalities in a 1:1 stoichiometric relationship. Using a cold-shock expression system, highly concentrated construct can be obtained from standard culture volumes while retaining essentially native protein activity. The fusion construct can be included in a standard target-bridged assay design for the sensitive detection of miRNA targets |
763859 |
1.13.12.5 | analysis |
establishment and evaluation of an indirect autophagy flux assay based on monitoring the degradation of an autophagosome-associated fusion protein Rluc-LC3 by luminescence detection. The Rluc-LC3 assay is useful for the identification of genes, miRNAs, and small molecules that regulate autophagy flux in mammalian cells |
745694 |
1.13.12.5 | analysis |
for analysis of the Hsp90 chaperone activity in complex with cochaperone Cdc37, split Renilla luciferase protein fragment-assisted complementation bioluminescence can be utilized to study the full-length human Hsp90-Cdc37 complex and to identity critical residues and their contributions for Hsp90/Cdc37 interaction in living cells |
712443 |
1.13.12.5 | analysis |
luciferase can be functionally expressed in Staphylococcus aureus and can be used as a biosensor for the agr quorum sensing system which employs autoinducing peptides to control virulence. Luciferase is linked to the P3 promoter of the agr operon and biosensor strains are validated by evaluation of chemical agent-mediated activation and inhibition of agr. Use of Luciferase enables quantitative assessment of agr activity |
765836 |
1.13.12.5 | analysis |
Renilla luciferase is a bioluminescent enzyme which is broadly used as a reporter protein in molecularbiosensors |
744813 |
1.13.12.5 | analysis |
Renilla luciferase is used in assay development for measurement of mitochondrial fusion, quantification via split-Renilla luciferase complementation in HeLa cells, validation of the Renilla luciferase reporter system for mitochondrial fusion, overview |
712977 |
1.13.12.5 | analysis |
the use of control Renilla luciferase vectors as normalizers requires that they not be influenced by any variables in the experiment. The zinc finger transcription factor WT1 effect on luciferase activation varies from no significant effect in 293 and PC3 cells to strong enhancement in LNCaP cells treated with the androgen analog R1881. Hormone enhances WT1-mediated activation of luciferase and these interactions require an intact WT1 zinc finger DNA binding domain |
686902 |