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Literature summary for 1.13.12.5 extracted from
- FcUni-RLuc an engineered Renilla luciferase with Fc binding ability and light emission activity (2015), Analyst, 140, 1438-1441 .
Application
| Application | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Renilla reniformis | |
| 0.0025 | - |
coelenterazine | wild-type enzyme, pH 7.2, 25°C | Renilla reniformis |  |
| 0.003 | - |
coelenterazine | modified enzyme FcUni-RLuc, pH 7.2, 25°C | Renilla reniformis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| coelenterazine + O2 | Renilla reniformis | - |
coelenteramide + CO2 + hv | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Renilla reniformis | P27652 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant soluble His6-tagged enzyme FcUni-RLuc from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography | Renilla reniformis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| coelenterazine + O2 | - |
Renilla reniformis | coelenteramide + CO2 + hv | - |
? | |
| 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 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 36000, recombinant His-tagged enzyme FcUni-RLuc, SDS-PAGE | Renilla reniformis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Renilla luciferase | - |
Renilla reniformis |
| RLuc | - |
Renilla reniformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Renilla reniformis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Renilla reniformis |
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Release 2023.1 (January 2023)
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