Bacterial synthesis of truncated forms of the human vitamin D and characterization of anti-receptor monoclonal antibodies

J. Schaefer-Klein, J. M. Londowski, Rajiv Kumar

Research output: Contribution to journalArticle

3 Scopus citations


We biosynthesized full-length (amino acids 1-427) and truncated human 1,25-dihydroxyvitamin D3 receptor proteins that encompassed only the putative DNA binding domain (amino acids 1-112) or the DNA binding domain and parts of the sterol binding domain (amino acids 1-193 and 1-328) in a bacterial expression system. We also prepared monoclonal antibodies against the full-length vitamin D receptor. The binding properties of the monoclonal antibodies were characterized by their ability to bind to full-length and trucated vitamin D receptor protein constructs. Seven of twelve monoclonal antibodies recognized the full-length receptor protein. These antibodies bound to truncated hVDR proteins with decreasing affinities as successive truncations were made from the carboxy-terminal end of the receptor protein. The five remaining monoclonal antibodies recognized the full-length and truncated receptor proteins with equally low affinities. Truncated forms of the vitamin D receptor and region-specific antibodies will be useful in assessing the properties of the receptor.

Original languageEnglish (US)
Pages (from-to)167-172
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 1993


ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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