Multispecificity of a recombinant anti-ras monoclonal antibody

Schrader, John W. and McLean, Gary R. (2017) Multispecificity of a recombinant anti-ras monoclonal antibody. Journal of molecular recognition : JMR, 31:2 (2683). ISSN 1099-1352

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Abstract / Description

Recombinant monoclonal antibodies (Ab's) have widespread application as research tools, diagnostic reagents and as biotherapeutics. Whilst studying the cellular molecular switch protein m-ras, a recombinant monoclonal antibody to m-ras was generated for use as a research tool. Antibody genes from a single rabbit B cell secreting IgG to an m-ras specific peptide sequence were expressed in mammalian cells, and monoclonal rabbit IgG binding was characterized by ELISA and peptide array blotting. Although the monoclonal Ab was selected for specificity to m-ras peptide, it also bound to both recombinant full-length m-ras and h-ras proteins. The cross-reactive binding of the monoclonal Ab to h-ras was defined by peptide array blot revealing that the Ab showed preference for peptide sequences containing multiple positively charged amino acid residues. These data reinforce the concept of antibody multispecificity through multiple interactions of the Ab paratope with diverse polypeptides. They also emphasize the importance of immunogen and Ab selection processes when generating recombinant monoclonal Ab's.

Item Type: Article
Uncontrolled Keywords: polyreactivity, ras, recombinant monoclonal antibody, specificity
Subjects: 500 Natural Sciences and Mathematics > 570 Life sciences; biology
Department: School of Human Sciences
Depositing User: Gary Mclean
Date Deposited: 16 Nov 2017 09:22
Last Modified: 17 Oct 2019 11:03


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