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Characterization of Monoclonal Antibodies to Human Protein 1/Clara Cell 10 Kilodalton Protein
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Tetsuji Yamaguchi
Published/Copyright:
June 1, 2005
Abstract
Human protein 1/Clara cell Mr 10 000 protein consists of two identical subunits of seventy amino acid residues each. In the present study, eight clones of monoclonal antibodies against native protein 1 were prepared and their respective epitopes were immunochemically and immunohistochemically characterized using native protein 1, truncated recombinant protein 1 and synthesized peptides. Among the clones, three designated as TY-5, TY-7 and TY-8 recognized amino acid residues 7–16, residues 19–28, and residues 39–46, respectively, all of which comprise the hydrophobic cavity of protein 1, possibly associated with chemical binding function. With the exception of TY-4, the remaining clones recognized residues 61–68 which are exposed to solvent. The epitope of TY-4 remains undetermined. Proper selection and combination of clones and recombinant protein 1 may be useful for fundamental and clinical studies of protein 1.
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Published Online: 2005-06-01
Published in Print: 1999-06-01
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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