By Amersham Biosciences
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Elute with 3–5 ml diluted elution buffer. Collect fractions into tubes containing neutralization buffer. 8. Immediately re-equilibrate the column with 5 ml diluted binding buffer. Storage Wash media and columns with 20% ethanol (use approximately 5 column volumes for packed media) and store at +4 to +8 °C. Using Sepharose media coupled to native or recombinant protein A Protein A is derived from a strain of Staphylococcus aureus and contains five regions that bind to the Fc region of IgG. As an affinity ligand, protein A is coupled to Sepharose so that these regions are free to bind.
3) Mix gently for 1 hour at +4 °C. Precipitation of the immune complexes 1) Add 50 µl of prepared Protein A Sepharose 4 Fast Flow or Protein G Sepharose 4 Fast Flow suspension (50% slurry). 2) Mix gently for 1 hour at +4 °C. 3) Centrifuge at 12 000 x g for 20 seconds and save the pellet. 4) Wash the pellet three times with 1 ml lysis buffer and once with wash buffer. Centrifuge at 12 000 x g for 20 seconds between each wash and discard the supernatants. Be very careful when removing the supernatants to avoid loss of the immunocomplexes.
Table 13 shows a comparison of the relative binding strengths of protein A and protein G to different immunoglobulins. Information has been compiled from various publications. Binding strengths are tested with free protein A or protein G and can be used as guidelines to predict the binding behaviour to a protein A or protein G purification medium. However, when coupled to an affinity matrix, the interaction may be altered. For example, rat IgG1 does not bind to protein A, but does bind to Protein A Sepharose.
Antibody Purification by Amersham Biosciences