GST was fused on the N-terminus of the lysine 63 polyubiquitin chain binding domain of TAB2 encompassing amino acids 627-693. This fusion protein can be used for in vitro GST pulldown assays and for enrichment of cellular proteins conjugated with lysine 63 polyubiquitin chains in whole cell or tissue lysates. GST-TAB2 (NZF) can be precipitated using glutathione resin. After washing, GST-TAB2 (NZF) and its bound proteins can be eluted by a buffer containing 10 mM glutathione.

GST was fused on the N-terminus of the lysine 63 polyubiquitin chain binding domain of TAB2 encompassing amino acids 627-693. This fusion protein can be used for in vitro GST pulldown GST was fused on the N-terminus of the lysine 63 polyubiquitin chain binding domain of TAB2 encompassing amino acids 627-693. This fusion protein can be used for in vitro GST pulldown assays and for enrichment of cellular proteins conjugated with lysine 63 polyubiquitin chains in whole cell or tissue lysates. GST-TAB2 (NZF) can be precipitated using glutathione resin. After washing, GST-TAB2 (NZF) and its bound proteins can be eluted by a buffer containing 10 mM glutathione.
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Coomassie-stained SDS-PAGE Lane 1: Molecular weight markers Lane 2: 5 µg purified GST-TAB2(627-693)

Note: Dissolve 10 mM glutathione in a neutral buffer could drop pH to 3 - 4. Use 0.2 M NaOH to adjust pH back to neutral.