Abstract
Monoclonal antibodies (MAbs) were generated against recombinant human insulin-like growth factor 1 (IGF-1) by fusion of NS-1 myeloma cells with spleen cells from BALB/c X DBA mice immunised with recombinant IGF-1 and synthetic peptide sequences derived from the published amino acid sequence of IGF-1. MAbs were produced that recognised four distinct epitopes including two defined segments of the C and D domains. All MAbs were IgM mouse immunoglobulins. These results indicate the feasibility of producing MAbs to highly conserved proteins.
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