Work

Single-step purification of full-length human androgen receptor

Year: 2005

Type: article

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.

Source: Nuclear Receptor Signaling

DOI: 10.1621/nrs.03001

Authors: Dalia Juzumiene, Ching-yi Chang, Daju Fan, Tanya Hartney, John D. Norris, Donald P. McDonnell

Institution: Duke Medical Center

Language: English

Topic: Biotin and Related Studies

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Funders: National Cancer Institute, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: G2376949011, G5067066281