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Molecular Basis for Species and Ligand Specificity of a Monoclonal Antibody Raised Against Human IGF-I

Department of Pediatrics, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599

Address all correspondence and requests for reprints to: Judson J. Van Wyk, M.D., University of North Carolina, Department of Pediatrics, School of Medicine, 509 Clinical Science Building, CB# 7220, Chapel Hill, North Carolina 27599.

	Abstract

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The anti-hIGF-I monoclonal antibody, -sm1.2, was found to have substantial crossreactivity with human and rat IGF-II, but recognized rat IGF-I only when this ligand was present at very high concentration. (E₅₀ for hIGF-I 3.5 ng/tube vs. 12,000 ng/tube for rat IGF-I). In the context of previous studies to define the epitope(s) of -sm1.2, these findings point to the critical importance of aspartic acid at residue 20 in the B domain in determining the species and ligand specificity of this antibody. Previous studies using this antibody in rodent tissues may require reinterpretation in the light of these findings.

Received July 30, 1997.

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