Studies with antibodies against the conserved cysteine region of progesterone receptor

David F. Smith, Daniel J. McCormick, David O. Toft

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1-7
Number of pages7
JournalJournal of Steroid Biochemistry
Volume30
Issue number1-6
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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