New PDF release: affinity chromatography principles and methods

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25. Purification of recombinant proteins on HiTrap Chelating HP, 5 ml, charged with Zn2+. Recombinant protein expressed in inclusion bodies Sample: 8 ml cell extract containing (His)10-tagged protein. The clone was a kind gift from Dr. C. Fuller and S. Brasher, Department of Biochemistry, University of Cambridge, UK. 4 Flow: Approx. 4 ml/min Equipment: Syringe Electrophoresis: SDS-PAGE, PhastSystem, PhastGel 10–15, 1 µl sample, silver staining Purification in 8 M urea Mr 97 000 66 000 45 000 30 000 20 100 14 400 1 2 3 4 5 6 7 Lane 1.

6. Wash the column with 7 column volumes of wash buffer. 7. Immediately re-equilibrate the column with 5 column volumes of binding buffer. 5 M) can be used instead of ammonium sulphate. 8 M ammonium sulphate. Some monoclonal IgMs may bind too tightly to the column for complete elution in binding buffer. The remaining IgM will be eluted with wash buffer, but the high content of isopropanol will cause precipitation of IgM. Perform an immediate buffer exchange (see page 133) or dilute the sample to preserve the IgM.

18a. Purification of a monoclonal IgG2a from clarified cell culture on rProtein A Sepharose 4 Fast Flow. Fig. 18b. SDS-PAGE of starting material (lane 2) and eluate (lane 3). The samples were concentrated 10 times and reduced. Lane 1 and 4 are LMW markers. PhastSystem, PhastGel Gradient 10–15. 0 Centrifuge samples (10 000 g for 10 minutes) to remove cells and debris. 45 µm filter. If needed, adjust sample conditions to the pH and ionic strength of the binding buffer either by buffer exchange on a desalting column (see page 133) or by dilution and pH adjustment.

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affinity chromatography principles and methods by GE HEalthcare


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