Abstract
Antibodies of the IgM class are elaborated by many common murine hybridoma cell lines and often define important antigens. In contrast to IgG antibodies, however, IgM molecules exhibit little or no affinity for bacterial Ig binding proteins, such as protein A and protein G, which are almost universally used to detect and/or bind IgG antibodies in cytofluorography, Western transfer, immunoprecipitation, and so forth. It is therefore highly desirable, in laboratories in which hybridoma technology is routine, to have in place a means of detecting and purifying IgM molecules, sometimes on a modest or large scale. The most efficacious and general method for IgM detection and purification still involves the appropriate use of heterospecific antimurine IgM antibodies.
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References
Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.
Walker, I. D. and Harris, A. W. (1980) Immunoglobulin Cμ RNA in T lymphoma cells is not translated. Nature 288, 290–293.
Walker, I. D. and Harris, A. W. (1981) μ polypeptide phenotypes of lymphoid and myeloid cell lines containing RNA transcripts of the immunoglobulin Cμ gene. J. Immunol. 127, 561–567.
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© 1995 Humana Press Inc.
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Walker, I.D. (1995). Detection, Purification, and Utilization of Murine Monoclonal IgM Antibodies. In: Davis, W.C. (eds) Monoclonal Antibody Protocols. Methods in Molecular Biology™, vol 45. Humana Press. https://doi.org/10.1385/0-89603-308-2:183
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DOI: https://doi.org/10.1385/0-89603-308-2:183
Publisher Name: Humana Press
Print ISBN: 978-0-89603-308-5
Online ISBN: 978-1-59259-532-7
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