Abstract
The Epstein-Barr viral nuclear antigen 2 (EBNA2) plays a key role during establishment and maintenance of B-cell immortalization after Epstein-Barr virus (EBV) infection (). EBNA2 acts as a transcriptional activator of cellular and viral genes (, , , , , , ) and is tethered to EBNA2 responsive promoter elements by interaction with a cellular DNA binding protein (,). We purified this transcription factor by classical chromatographic methods, however, instead of the usual final DNA affinity column step, we applied a magnetic DNA affinity purification protocol. This increased the purity of the transcription factor from about 0.01% to almost homogeneity and allowed subsequent identification of the protein as RBP-Jκ ().
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