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) |
|---|---|
| Pages (from-to) | 167-172 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 196 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1993 |
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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 journal › Article
}
TY - JOUR
T1 - Bacterial synthesis of truncated forms of the human vitamin D and characterization of anti-receptor monoclonal antibodies
AU - Schaefer-Klein, J.
AU - Londowski, J. M.
AU - Kumar, Rajiv
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0027501130&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027501130&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1993.2230
DO - 10.1006/bbrc.1993.2230
M3 - Article
C2 - 7692846
AN - SCOPUS:0027501130
VL - 196
SP - 167
EP - 172
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -