Studies with antibodies against the conserved cysteine region of progesterone receptor.
Polyclonal antibodies were generated against two synthetic peptides corresponding to sequences from the DNA-binding domain of steroid receptors. The sequence for peptide 1 (13 amino acids) lies between the two putative metal-binding loops of the conserved cysteine region while the sequence for peptide 2 (12 amino acids) lies within one loop. Peptide antibodies were generated by injecting rabbits with peptide conjugated to bovine serum albumin. By Western blot analysis, antibodies to peptide 2 recognized chick and human progesterone receptor and human glucocorticoid receptor, but peptide 1 antibodies did not. No cross-reactivity with native chick progesterone receptor was detected with either anti-peptide. These findings suggest that the epitopes for peptide 2 antibodies, and possibly for peptide 1 antibodies, are inaccessible to antibody in the native receptor.
Smith
D F
DF
Department of Biochemistry and Molecular Biology, Mayo Medical School, Rochester, MN 55905.
McCormick
D J
DJ
Toft
D O
DO
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002645:Chickens; D003600:Cytosol / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D005260:Female; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D010057:Oviducts / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D011980:Receptors, Progesterone / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D014599:Uterus / Q000378:metabolism
D000906:Antibodies; D010446:Peptide Fragments; D011980:Receptors, Progesterone; D004247:DNA