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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 251))

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Abstract

Immunization with a foreign antigen causes B cells of the immune system to produce antibodies of exquisite specificity toward the challenging antigen. This specific reactivity has made antibodies an essential tool for the detection and purification of protein in all fields of biological research. IgG is the most predominant class of serum antibody and is an integral part of many applications within the laboratory. The need to purify monoclonal or polyclonal antibodies is largely determined by the intended application of the antibody. Unpurified antibody is well suited to use in indirect flow cytometry assays, most enzyme-linked immunosorbent assays (ELISAs), for cytotoxicity assays or Western blot analyses. Purified antibody must be used, however, when accurate concentrations are required, chemical modifications such as labeling with fluorescent or radioactive probes are needed, when fragmentation of the antibody is required for binding or crystallization analysis or when antibody is directly coupled to a matrix for immunoaffinity chromatography.

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© 2004 Humana Press Inc.

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Powell, M.S., Wines, B.D. (2004). IgG Purification. In: Aguilar, MI. (eds) HPLC of Peptides and Proteins. Methods in Molecular Biology™, vol 251. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-742-4:341

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  • DOI: https://doi.org/10.1385/1-59259-742-4:341

  • Publisher Name: Springer, Totowa, NJ

  • Print ISBN: 978-0-89603-977-3

  • Online ISBN: 978-1-59259-742-0

  • eBook Packages: Springer Protocols

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