EC Number | Application | Comment | Organism |
---|---|---|---|
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 | Renilla reniformis |
1.13.12.5 | biotechnology | 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 | Renilla reniformis |
1.13.12.5 | molecular biology | 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 | Renilla reniformis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.12.5 | recombinant expression of soluble His6-tagged enzyme FcUni-RLuc in Escherichia coli strain BL21 (DE3), an Fc-binding peptide is separated by a five-amino acid linker from RLuc | Renilla reniformis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.12.5 | additional information | - |
additional information | Michaelis-Menten kinetics | Renilla reniformis | |
1.13.12.5 | 0.0025 | - |
coelenterazine | wild-type enzyme, pH 7.2, 25°C | Renilla reniformis | |
1.13.12.5 | 0.003 | - |
coelenterazine | modified enzyme FcUni-RLuc, pH 7.2, 25°C | Renilla reniformis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.5 | coelenterazine + O2 | Renilla reniformis | - |
coelenteramide + CO2 + hv | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.12.5 | Renilla reniformis | P27652 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.12.5 | recombinant soluble His6-tagged enzyme FcUni-RLuc from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography | Renilla reniformis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.5 | coelenterazine + O2 | - |
Renilla reniformis | coelenteramide + CO2 + hv | - |
? | |
1.13.12.5 | additional information | dynamic light scattering has been used for the detection of protein-protein interaction between the IgG antibody and modified enzyme FcUni-RLuc, to which an Fc-binding peptide is bound and separated by a five-amino acid linker from RLuc. Analysis of FcUni-RLuc and Herceptin interaction | Renilla reniformis | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.12.5 | ? | x * 36000, recombinant His-tagged enzyme FcUni-RLuc, SDS-PAGE | Renilla reniformis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.12.5 | Renilla luciferase | - |
Renilla reniformis |
1.13.12.5 | RLuc | - |
Renilla reniformis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.13.12.5 | 25 | - |
assay at | Renilla reniformis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.12.5 | 7.2 | - |
assay at | Renilla reniformis |