By Amersham Biosciences
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Extra resources for Antibody Purification
Relative binding strengths of protein A or protein G. Single-step purification based on Fc region specificity will co-purify host IgG and may even bind trace amounts of serum proteins. To avoid trace amounts of contaminating IgG, consider alternative techniques such as immunospecific affinity (using anti-host IgG antibodies as the ligand to remove host IgG or target specific antigen to avoid binding host IgG), ion exchange or hydrophobic interaction chromatography (see Chapter 6). Both protein A and a recombinant protein A are available, with similar specificities for the Fc region of IgG.
2. Inject 3 × 2 column volumes of wash buffer. 3. Inject 3 × 2 column volumes of blocking buffer. 4. Let the column stand for 15–30 min. 5. Inject 3 × 2 column volumes of wash buffer. 6. Inject 3 × 2 column volumes of blocking buffer. 7. Inject 3 × 2 column volumes of wash buffer. 8. Inject 2–5 column volumes of a buffer with neutral pH. The column is now ready for use. A HiTrap column can be used with a syringe, a peristaltic pump or connected to a liquid chromatography system, such as ÄKTAprime.
4. Wash with 5–10 column volumes of binding buffer, or until no material appears in the eluent as monitored by absorption at A280. 5. Elute with 1–3 column volumes of elution buffer (larger volumes may be necessary). 6. If required, purified fractions can be desalted and transferred into the buffer of choice using prepacked desalting columns (see page 21). 7. Re-equilibrate the column immediately by washing with 5–10 column volumes of binding buffer. Avoid excessive washing if the interaction between the protein of interest and the ligand is weak, since this may decrease the yield.