A Method for the Rapid and Efficient Elution of Native Affinity-Purified Protein A Tagged Complexes
| Autor: | Jaclyn Tetenbaum-Novatt, Brian T. Chait, Brian S. Imai, Caterina Strambio-De-Castillia, Michael P. Rout |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Proteomics
Staphylococcus aureus Time Factors Recombinant Fusion Proteins Biotin Peptide Biology Biochemistry Chromatography Affinity Structural genomics Sepharose Bacterial Proteins Staphylococcus aureus protein A chemistry.chemical_classification Chromatography Temperature Proteins General Chemistry Hydrogen-Ion Concentration Fusion protein Models Chemical chemistry Immunoglobulin G biology.protein Protein G Peptides Protein A |
| Zdroj: | Journal of Proteome Research. 4:2250-2256 |
| ISSN: | 1535-3907 1535-3893 |
| Popis: | A problem faced in proteomics studies is the recovery of tagged protein complexes in their native and active form. Here we describe a peptide, Bio-Ox, that mimics the immunoglobulin G (IgG) binding interface of Staphylococcus aureus Protein A, and competitively displaces affinity-purified Protein A fusion proteins and protein complexes from IgG-Sepharose. We show that Bio-Ox elution is a robust method for the efficient and rapid recovery of native tagged proteins, and can be applied to a variety of structural genomics and proteomics studies. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|