Monoclonal Antibodies to Human Vitamin D-Binding Protein

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 82; no. 24; pp. 8429 - 8433
• Main Authors: Pierce, Eric A., Dame, Margaret C., Bouillon, Roger, Van Baelen, Hugo, DeLuca, Hector F.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01-12-1985; National Acad Sciences
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Antibodies; Antibodies, Monoclonal - immunology; Antibody Specificity; Antiserum; Binding and carrier proteins; Biochemistry; Biological and medical sciences; Biotechnology; Chickens; Cross Reactions; Enzyme linked immunosorbent assay; Fundamental and applied biological sciences. Psychology; Gels; Haplorhini; Health. Pharmaceutical industry; Humans; Hybridomas; Hybridomas - immunology; Immunoprecipitation; Industrial applications and implications. Economical aspects; Mice; Monoclonal antibodies; Production of active biomolecules; Proteins; Rats; Serum albumins; Space life sciences; Species Specificity; Swine; Ungulates; Vitamin D-Binding Protein - immunology; Human; Binding protein; Monoclonal antibody; Vitamin D; Production
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.82.24.8429

Monoclonal antibodies to vitamin D-binding protein isolated from human serum have been produced. The antibodies obtained have been shown to be specific for human vitamin D-binding protein by three independent assays. The antibodies recognize human vitamin D-binding protein specifically in an enzyme-linked immunosorbent assay. Human vitamin D-binding protein is detected specifically in both pure and crude samples by a radiometric immunosorbent assay (RISA) and by an immunoprecipitation assay. The anti-human vitamin D-binding protein antibodies cross-react with monkey and pig vitamin D-binding protein, but not with vitamin D-binding protein from rat, mouse, or chicken, as determined by the RISA and immunoprecipitation assays.