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45 µm HiTrap NHS-activated HP 1 ml. , recycled with a peristaltic pump for 1 h. 5 mg). 0 1 SDS-PAGE. PhastSystem. PhastGel Gradient 8–25 1 µl sample, Coomassie stained 20 Fig. 22. Purification of anti-mouse Fc-IgG from sheep antiserum. 46 30 000 20 100 Binding Elution buffer buffer 40 60 80 100 ml 2 Lane 1: Desorbed material, non-reduced Lane 2: Low Molecular Weight Calibration Kit, reduced Preparing NHS-activated media Product Comments HiTrap NHS-activated HP Pre-activated medium for coupling via primary amine group of a ligand.

1. Equilibrate the column with 5 column volumes of binding buffer. 2. Apply sample. 3. Wash with 5–10 column volumes of the binding buffer to remove impurities and unbound material. Continue until no protein is detected in the eluent (determined by UV absorbance at 280 nm). 4. Elute with 5 column volumes of elution buffer**. 5. Re-equilibrate with 5–10 column volumes of binding buffer. 0 per ml fraction), so that the final pH of the fractions will be approximately neutral. Table 14 gives examples of some typical binding and elution conditions that have been used with Protein A Sepharose.

Dilution of the fractionated sample or rapid buffer exchange using a desalting column will prepare it for the next IEX or AC step. Gel filtration is a non-binding technique unaffected by buffer conditions, but with limited volume capacity. GF is well suited for use after any of the concentrating techniques (IEX, HIC, AC, EBA) since the target protein will be eluted in a reduced volume and the components from the elution buffer will not affect the gel filtration process.

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Antibody Purification by Amersham Biosciences


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