Characterization of a cathepsin D protease from CHO cell-free medium and mitigation of its impact on the stability of a recombinant therapeutic protein
Author:
Affiliation:
1. Bioproduct Research and Development, Eli Lilly and Company; Indianapolis IN 46285
Publisher
Wiley
Subject
Biotechnology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.2530/fullpdf
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2. Of [Hamsters] and men: a new perspective on host cell proteins;Gutiérrez;Hum Vaccin Immunother.,2012
3. Degradation of an Fc-fusion recombinant protein by host cell proteases: identification of a CHO cathepsin D protease;Robert;Biotechnol Bioeng.,2009
4. Characterization of the proteases involved in the N-terminal clipping of glucagon-like-peptide-1-antibody fusion proteins;Dorai;Biotechnol Prog.,2011
5. Fragmentation of a highly purified monoclonal antibody attributed to residual CHO cell protease activity;Gao;Biotechnol Bioeng.,2011
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