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 language | English (US) |
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Pages (from-to) | 167-172 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 196 |
Issue number | 1 |
DOIs | |
State | Published - 1993 |
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology