As the pharmaceutical industry pipeline continues to shift from traditional, small-molecule-based drugs to a new class of biologic therapeutics, bioresearchers need powerful bioanalytical techniques for the in-depth characterization of the protein of interest required at each developmental stage.
Meet your quality goals and exceed your cost reduction objectives in 2012. Learn the latest about Nuvia™ Q and Nuvia S high capacity ion exchange media by attending Bio-Rad's technical session at BioProcess International Europe, April 18 and 19, 2012 in Prague. Stop by the Bio-Rad Booth 37 and 42 to explore new purifications schemes that make the most of mixed-mode chromatography for robust intermediate and final polish for antibodies and other molecules. Learn more.
Characterization Of Human Immunoglobulin G Binding Peptides
By Hatanaka Takaaki, Kakoi Sayaka, Ito Yuji, Kagoshima University, and Laura Moriarty, Bio-Rad Laboratories, Inc.
Human immunoglobulin G (hIgG) is a major immunoglobulin in serum that plays a central role in immune response. There is great interest in the use of hIgGs in basic biomedical research, and for the diagnosis and treatment of various diseases. Immunoglobulins (Ig) are usually purified by Protein A affinity chromatography.
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