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. 2014 Jan 29;9(4):493–500. doi: 10.1002/biot.201300207

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© 2013 The Authors. Biotechnology Journal published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

This is an open access article under the terms of the Creative Commons Attribution-License, which permits use and distribution in any medium, provided the original work is properly cited.

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Processing of 2F5 by serine and cysteine proteinases. CHO-derived 2F5 (200 ng) was incubated with selected proteinases (10 ng) at pH 5.5 for the indicated times and then analyzed by immunoblotting with antibodies to the heavy chain of human IgG. Untreated antibody was used as control. CathB, cathepsin B; CathL, cathepsin L. The migration positions of selected molecular mass standards are indicated, with their respective masses expressed in kDa. The results shown are representative of at least two independent experiments.