کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2021372 1069243 2008 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Expression, purification, and characterization of multiple, multifunctional human glucocorticoid receptor proteins
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Expression, purification, and characterization of multiple, multifunctional human glucocorticoid receptor proteins
چکیده انگلیسی

The glucocorticoid receptor (GR) is a nuclear receptor protein that plays a central role in glucose homeostasis, the stress response, control of the hypothalamic-pituitary-adrenal axis, and immuno-inflammatory processes via binding of the natural steroid, cortisol. GR is a well-validated drug target and continues to be an important target for new drug discovery efforts. Here, we describe a basic and simple method for Escherichia coli expression and purification of a variety of human GR proteins that contain all three of the functional domains of the protein: the activation function-1 domain, the DNA-binding domain, and the ligand-binding domain. We present characterization data to show that these purified, multifunctional GR proteins are active for ligand, coactivator, and DNA-binding. The work presented here should serve as a reference for future mechanistic, structural and drug discovery efforts that require purified, full or near full length, GR protein.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 62, Issue 1, November 2008, Pages 29–35
نویسندگان
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