title: Single-step purification of full-length human androgen receptor.
abstract: 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.
authors.affiliation: Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
authors.forename: Dalia
authors.initials: D
authors.lastname: Juzumiene
authors.forename: Ching-yi
authors.initials: CY
authors.lastname: Chang
authors.forename: Daju
authors.initials: D
authors.lastname: Fan
authors.forename: Tanya
authors.initials: T
authors.lastname: Hartney
authors.forename: John D
authors.initials: JD
authors.lastname: Norris
authors.forename: Donald P
authors.initials: DP
authors.lastname: McDonnell