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Purification of recombinant human interferon lambda 4. (A) Refolded IFNλ4 was loaded on an anion exchange column (5 ml Hi trap SP FF). The protein was eluted from the column using a salt gradient and the fractions of the peak at ≈10 ml were collected. (B) The fractions collected from the ion exchange column were applied to a gelfiltration column (Hi load Superdex 75). The fractions around the peak at≈75 ml were pooled. (C) A Coomassie stained 12% SDS–PAGE gel of the purified protein.
