VDR-LBD - Vitamin D Receptor Ligand Binding Domain (118-427)

• Species: Human
• Expression Host: E.coli
• Tag: His-tag
• Purity: 90%
• Molecular Weight: 37.1 kDa.
• Gene Accession Number: NM_000376.

Purification and Quality Control
The His-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns.
The purified VDR-LBD is greater than 95% homogeneous based on SDS-PAGE analysis.

Unit Definition (Activity)
1 unit equals 1 nanogram of purified protein. 1 unit is sufficient for a gel mobility shift assay in a 20 µl reaction; 100 units are sufficient for protein-protein interaction assays.

Applications
Recombinant VDR-LBD can be used for: ligand binding assays.

Formulation and Storage
The protein is in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol. Stored at -70°C before use. Avoid repeated freeze thaw cycles.

Synonym
vitamin D (1,25- dihydroxyvitamin D3) receptor and NR1I1.

Protein Sequence
DSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVN DGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVT LELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSN ESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLM AICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRS LNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS

Background
The vitamin D endocrine system is critical for the proper development and maintenance of mineral ion homeostasis and skeletal integrity (1). Beyond these classical roles, recent evidence suggests that the bioactive metabolite of vitamin D, 1,25-dihydroxyvitamin D3, functions in diverse physiological processes, such as hair follicle cycling, blood pressure regulation, and mammary gland development (2). The biological effects of 1,25-(OH)2D3 are mediated through the vitamin D receptor (VDR), a member of the nuclear receptor superfamily of ligand-activated transcription factors (3). The cellular effects of VDR signaling include growth arrest, differentiation and/or induction of apoptosis. VDR heterodimerizes with RXR and the liganded VDR-RXR heterodimer binds with high affinity to vitamin D response elements (VDREs) in the promoters of target genes (4). In addition, several nuclear receptor coactivators (SRC-1, DRIP) have been shown to interact with VDR and potentiate its transcriptional activity (5-7). In addition to treating disorders of mineral metabolism and diseases of the skeleton, such as rickets, osteoporosis, and renal osteodystrophy, VDR and 1,25-(OH)2D3 have significant therapeutic potential for pathologies such as cancer, autoimmune syndromes, and psoriasis.

Image of SDS-PAGE /Western-blot