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Extra resources for Affinity Chromatography: Principles and Methods
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. GST fusion proteins GST MicroSpin Purification Module, GSTrap FF, GSTPrep FF 16/10, Glutathione Sepharose 4 Fast Flow, Glutathione Sepharose 4B Glutathione S-transferase (GST) is one of the most common tags used to facilitate the purification and detection of recombinant proteins and a range of products for simple, one step purification of GST fusion proteins are available (see Purification options).
5 with 30% isopropanol The sample must have the same concentration of ammonium sulphate as the binding buffer. 8 M. Stir slowly and continuously. 45 µm filter immediately before applying it to the column. 8 M ammonium sulphate. 0 M. To avoid precipitation of IgM, it is important to add the ammonium sulphate slowly. An increased concentration of ammonium sulphate will cause more IgG to bind, which might be a problem if serum has been added to the cell culture medium. If there is IgG contamination of the purified IgM, the IgG can be removed by using HiTrap Protein A HP, HiTrap rProtein A FF, or HiTrap Protein G HP.
44 1: 2: 3: 4: 5: 6: 7: 8: 9: 10: Low Molecular Weight (LMW) calibration kit, reduced Extract of E. coli expressing GST-DemA, 1 g cell paste/5 ml Flow-through from GSTrap FF 1 ml GST-DemA eluted from GSTrap FF 1 ml Extract of E. coli expressing GST-DemA, 1 g cell paste/5 ml Flow-through from GSTrap FF 5 ml GST-DemA eluted from GSTrap FF 5 ml Extract of E. 0 A B C Fig. 24. Using GSTrap FF with a syringe. A: Prepare buffers and sample. Remove the column’s top cap and twist off the end. B: Equilibrate column, load the sample and begin collecting fractions.