protein

Vitamin D Receptor/VDR Protein, Human (sf9, His)

HY-P73543

5 μg;10 μg;50 μg;100 μg

72;115;320;510 USD

Vitamin D Receptor/VDR Protein, Human (sf9, His)

proteins

Sf9 insect cells

5 μg;10 μg;50 μg;100 μg

72;115;320;510 USD

Vitamin D receptor (VDR) acts as a nuclear receptor for calcitriol, the active form of vitamin D3, triggering cellular effects. After vitamin D3 binding, VDR translocates to the nucleus and forms a heterodimer with the retinoid X receptor (RXR). Vitamin D Receptor/VDR Protein, Human (sf9, His) is the recombinant human-derived Vitamin D Receptor/VDR protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of Vitamin D Receptor/VDR Protein, Human (sf9, His) is 427 a.a., with molecular weight of ~50 kDa.

Human

The Vitamin D Receptor (VDR) functions as a nuclear receptor for calcitriol, the active form of vitamin D3, mediating its cellular effects. Upon binding to vitamin D3, VDR translocates to the nucleus and forms heterodimers with the retinoid X receptor (RXR). These VDR-RXR heterodimers bind to specific response elements on DNA, activating the transcription of target genes responsive to vitamin D3. Beyond its role in calcium homeostasis, VDR also serves as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites. In the absence of bound vitamin D3, VDR exists as a homodimer, and upon binding, it forms a heterodimer with RXRA. VDR interacts with various coactivators, including MED1, NCOA1, NCOA2, NCOA3, and NCOA6, leading to increased transcription of target genes. Additionally, VDR interacts with the corepressor NCOR1 and SNW1. It forms ligand-dependent interactions with CRY1 and CRY2, and also interacts with IRX4 without affecting its transactivation activity.

Vitamin D3 receptor; VDR; NR1I1

Greater than 88% as determined by reducing SDS-PAGE.

Supplied as a 0.2 μm filtered solution of 20 mM Tris, 100 mM NaCl, pH 8.0, 10% Glycerol.

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