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 Citations (Scopus)

Abstract

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
Volume196
Issue number1
DOIs
StatePublished - 1993

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Vitamin D
Calcitriol Receptors
Monoclonal Antibodies
Proteins
Amino Acids
Antibodies
DNA
Sterols

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Bacterial synthesis of truncated forms of the human vitamin D and characterization of anti-receptor monoclonal antibodies. / Schaefer-Klein, J.; Londowski, J. M.; Kumar, Rajiv.

In: Biochemical and Biophysical Research Communications, Vol. 196, No. 1, 1993, p. 167-172.

Research output: Contribution to journalArticle

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