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

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.

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.

Human

Sf9 insect cells

C-His

P11473 (M1-S427)

7421  [NCBI]

Approximately 50 kDa

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

<1 EU/μg, determined by LAL method.