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Expression and Purification of Recombinant Human Progesterone Receptor in Baculovirus and Bacterial Systems

  • Vida Senkus Melvin
  • Dean P. Edwards
Part of the Methods in Molecular Biology™ book series (MIMB, volume 176)

Abstract

Human progesterone receptor (PR) is a member of the nuclear hormone receptor superfamily of transcriptional activators, which share a common modular structure consisting of a C-terminal ligand-binding domain (LBD), a highly conserved and centrally located DNA-binding domain (DBD), and a poorly characterized N-terminal domain that is required for maximal transcriptional activity (1,2) Human PR is expressed as two proteins from a single gene by alternate use of two promoters: PR-A, which is missing the first 164 amino acids in the N-terminus, and full-length PR-B (3).

Keywords

Progesterone Receptor Nonspecific Protein Binding Human Progesterone Receptor Ptac Promoter Enterokinase Cleavage Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc. 2001

Authors and Affiliations

  • Vida Senkus Melvin
    • 1
  • Dean P. Edwards
    • 1
  1. 1.Department of PathologyUniversity of ColoradoHealth Sciences CenterDenver

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