Characterization of a monoclonal antibody to human erythropoietin.

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Abstract
Hybrid cells that synthesize a monospecific antibody directed toward erythropoietin were produced by the fusion of mouse plasmacytoma cells with spleen cells from rats immunized against human erythropoietin. The antibody bound the .alpha. and .beta. forms and the asialo .alpha. form of erythropoietin to the same extent. It was an Ig of the IgG class and bound only erythropoietin in an impure preparation of the hormone. Biologically active unlabeled erythropoietin competed with biologically inactive radiolabeled hormone for monoclonal antibody binding sites. The biological activity of erythropoietin measured in vitro was not inactivated when it was bound by the monoclonal antibody.