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将雄激素受体（ＡＲ）的ｃＤＮＡ１１１９ｂｐ片段（１１０５～２２２４）（其中包含其ＤＮＡ结合结构域到部分激素结合结构域）克隆于表达质粒ｐＧＥＸ中，通过ＩＰＴＧ诱导，在Ｅ．ｃｏｌｉ中表达ＧＳＴ－ＡＲ融合蛋白，经谷胱甘肽－Ｓｅｐｈａｒｏｓｅ－４Ｂ亲和层析得以部分纯化。利用一个有雄激素应答元件（ＡＲＥ）活性的Ｃ３（１）ＤＮＡ片段为阳性探针，通过凝胶阻滞分析和ＤＮａｓｅＩ足迹法证明此表达产物具有特异的ＤＮＡ结合活性。
The cDNA 1119 bp fragment (1105-2224) of the androgen receptor (AR), including its DNA binding domain to the partial hormone binding domain, was cloned into the expression plasmid pGEX, induced by IPTG, in E. coli. The GST-AR fusion protein was expressed in E. coli and partially purified by glutathione-Sepharose 4B affinity chromatography. A C3 (1) DNA fragment with activity of androgen responsive element (ARE) was used as a positive probe. The gel block analysis and DNaseI footprinting demonstrated that the expressed product had specific DNA binding activity.