By Amersham Biosciences
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Extra resources for Affinity Chromatography
GSTrap FF columns can be used with a syringe, a peristaltic pump or a chromatography system. Enzyme-specific recognition sites are often included to allow the removal of the GST tag by enzymatic cleavage when required. Thrombin is commonly used for enzymatic cleavage, and must, subsequently, be removed from the recombinant product. HiTrap Benzamidine FF (high sub) 1 ml or 5 ml columns provide simple, ready-made solutions for this process (see page 54). Reuse of GSTrap FF depends on the nature of the sample.
Recombinant fusion proteins The purification of recombinant proteins can often be simplified by incorporating a tag of known size into the protein. As well as providing a marker for expression and facilitating detection of the recombinant protein, an important role for the tag is to enable a simple purification by affinity chromatography. The two most commonly used tags are glutathioneS-transferase (GST) and 6 x histidine residues (His)6. Protein A fusion proteins have also been produced to take advantage of the affinity between IgG and protein A for affinity purification.
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. * 5. Immediately 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. 35 Table 3 gives examples of some typical binding and elution conditions that have been used with Protein A Sepharose. Table 3. 0 3–4 (using thiocyanate) Binding strengths are tested with free protein A.