Application | Comment | Organism |
---|---|---|
analysis | reporter enzyme which is used for studies in higher plants because endogenous activities are low and sensitive assays are available. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus. This altered protein can be useful for promoter studies which require more rapid changes in the accumulation of the reporter protein | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the enzyme is engineered as fusion with an N-terminal 76 amino acid ubiquitin-coding region. When translated in any eukaryotic cell, such ubiquitin fusions are cleaved by ubiqitin-specific proteases specifically after the C-terminus of ubiquitin, irrespective of the distal amino acid (with the exception of Pro), releasing the downstream protein with the specified amino terminus. The presence of an N-terminal uncleavable ubiquitin on GUS does not reduce activity. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
beta-glucuronidase | - |
Escherichia coli |
GUS | - |
Escherichia coli |