Single-step purification of full-length human androgen receptor.

Published

Journal Article

The full-length human androgen receptor with an N-terminal biotin acceptor peptide tag was overexpressed in Spodoptera frugiperda cells in the presence of 1 microM dihydrotestosterone. Site-specific biotinylation of BAP was achieved in vivo by co-expression of E. coli biotin holoenzyme synthetase. The androgen receptor was purified by single-step affinity chromatography using Streptavidin Mutein Matrix under native conditions. The resultant protein was active, stable, 95% homogeneous, and we obtained sufficient yield for use in functional and structural studies.

Full Text

Duke Authors

Cited Authors

  • Juzumiene, D; Chang, C-Y; Fan, D; Hartney, T; Norris, JD; McDonnell, DP

Published Date

  • 2005

Published In

Volume / Issue

  • 3 /

Start / End Page

  • e001 -

PubMed ID

  • 16604169

Pubmed Central ID

  • 16604169

Electronic International Standard Serial Number (EISSN)

  • 1550-7629

Digital Object Identifier (DOI)

  • 10.1621/nrs.03001

Language

  • eng

Conference Location

  • United States