affinity chromatography principles and methods by GE HEalthcare PDF

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Lane 6. Lane 7. Lane 8. 75 Start refolding fr. fr. fr. 25 fr. 46 fr. 49 Start elution Manually using a syringe: • Sample loading • Gua-HCl wash • Urea wash 0 10 20 30 40 50 60 65 ml Low Molecular Weight Calibration Kit (LMW) Starting material for Lane 1. LMW HiTrap Chelating HP, 1 ml Lane 2. Fraction 38 Mr Fraction 1 Gua-HCl Lane 3. Fraction 39 wash (manually) Lane 4. Fraction 40 97 000 Fraction 2 Gua-HCl 66 000 Lane 5. Fraction 41 wash (manually) 45 000 Lane 6. Fraction 42 Fraction 3 Gua-HCl 30 000 Lane 7.

Pool I, purified Protein A-(HisGly)4His, reduced Fig. 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.

Protein A Sepharose 4 Fast Flow and rProtein A Sepharose 4 Fast Flow have a higher binding capacity, a more rigid matrix and provide more convenient alternatives to Protein A Sepharose CL-4B which must be rehydrated before column packing. Chemical stability These media and columns tolerate high concentrations of urea, guanidine HCl and chaotropic agents. Storage Wash media and columns with 20% ethanol (use approximately 5 column volumes for packed media) and store at +4 to +8 °C. 37 Monoclonal IgM from hybridoma cell culture HiTrap IgM Purification HP The technique described here is optimized for purification of monoclonal IgM from hybridoma cell culture, but it can be used as a starting point to determine the binding and elution conditions required for other IgM preparations.

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affinity chromatography principles and methods by GE HEalthcare


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