Article
Use of the Glu-Glu-Phe C-terminal epitope for rapid purification of the catalytic domain of normal and mutant ras GTPase-activating proteins.
The Journal of biological chemistry - 5 Aug 1991
Skinner R H, Bradley S, Brown A L, Johnson N J, Rhodes S, Stammers D K, Lowe P N
Abstract excerpt
The C-terminal catalytic domain (residues 704-1047) of the human ras GTPase-activating protein (GAP) has been engineered so as to incorporate the tripeptide, Glu-Glu-Phe, at its C terminus. This motif is recognized by the commercially available YL1/2 monoclonal antibody to alpha-tubulin and has p...
Topics
- Amino Acid Sequence
- Base Sequence
- Blotting, Western
- Catalysis
- Chromatography, Affinity
- Cloning, Molecular
- DNA
- Electrophoresis, Polyacrylamide Gel
- Epitopes
- Escherichia coli
- GTPase-Activating Proteins
- Gene Expression Regulation, Bacterial
- Molecular Sequence Data
- Mutation
- Polymerase Chain Reaction
- Proteins
- ras GTPase-Activating Proteins