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Production and purification of a PER.C&-Expressed IgM Antibody Therapeutic

C. Valasek, J. Cole, F. Hensel, P. Ye, M. A. Conner, M. E. Ultee

BioProcess International, Vol. 9, No. 11, December 2011, pp. 28–37

Immunoglobulin G (IgG) antibodies have been used to treat cancer for many years (1). Another class of antibodies—immunoglobulin M (IgM)—has been overlooked in spite of offering unique advantages that make them highly desirable as cancer therapeutics. Serving a valuable function in our innate immune system, IgM antibodies are the first to be secreted when an abnormal cell is present (2). These antibodies play a critical role in recognition and elimination of infectious particles (3,4), in removal of intracellular components, and in immunosurveillance mechanisms against malignant cells (5,6). IgMs also can bind to multiple copies of a target on a cancer cell surface. Such high avidity leads to cross-linking and more effective cell killing (7).

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