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

Vitamin D receptor (VDR) protein is the nuclear receptor of calcitriol, which translocates to the nucleus after binding vitamin D3, thereby coordinating cellular activities. VDR forms a heterodimer with RXR, binds to DNA response elements, and initiates the transcription of vitamin D3-responsive genes. Vitamin D Receptor/VDR Protein, Mouse (sf9, His) is the recombinant mouse-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, Mouse (sf9, His) is 422 a.a., with molecular weight of ~55 kDa.

Vitamin D Receptor (VDR) Protein serves as a nuclear receptor for calcitriol, the active form of vitamin D3, mediating its cellular actions. Upon binding vitamin D3, VDR translocates into the nucleus, forming heterodimers with the retinoid X receptor (RXR). The VDR-RXR heterodimers then bind to specific response elements on DNA, initiating the transcription of vitamin D3-responsive target genes. Beyond its central role in calcium homeostasis, VDR also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites. In the absence of bound vitamin D3, VDR forms homodimers, while vitamin D3 binding prompts heterodimerization with RXRA. VDR interacts with various coactivators, including MED1, NCOA1, NCOA2, NCOA3, and NCOA6, leading to enhanced transcription of target genes. It also interacts with the corepressor NCOR1, SNW1, IRX4, and exhibits ligand-dependent interactions with CRY1 and CRY2. These molecular interactions highlight the complex regulatory network that governs the transcriptional activity of VDR in response to vitamin D3 and other ligands.

Mouse

Sf9 insect cells

C-His

P48281 (M1-S422)

22337  [NCBI]

Approximately 55 kDa

Greater than 86% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.