Folding and purification of a recombinantly expressed interferon regulatory factor, IRF-4.

Interferon regulatory factor 4 (IRF-4), an intracellular, multidomain protein, is a member of the interferon regulatory factor family and a lymphoid-specific transcription factor that can form a ternary complex with DNA and the transcription factor PU.1. Recombinant human IRF-4 was expressed in Escherichia coli and purified from the soluble cell extract and the insoluble inclusion bodies.

Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody.

A monoclonal IgG-1 was produced by culture of a murine hybridoma (3.8.6) by three different methods, namely culture in ascites, in serum-free media and in serum-supplemented media.

The recovery of highly purified biopharmaceuticals from perfusion cell culture bioreactors.

The impact of continuous perfusion cell culture technology on production of one and two chain human rtPA, as well as monoclonal IgG and IgM, will be reviewed. Perfusion as compared to batch systems improve the quality of the product in the conditioned media in terms of biological activity and structural integrity. This significantly increases downstream recovery and daily production output of final purified material.