VDR Monoclonal Antibody (9A7), Invitrogen™

Description

MA1-710 detects vitamin D receptor (VDR) from human, rat, mouse, hamster, chicken, amphibian, and fish tissues. This antibody does not cross-react with estrogen or glucocorticoid receptors. MA1-710 detects both the occupied and unoccupied forms of the receptor. MA1-710 has been successfully used in Western blot, IF, ICC, IP, ChIP, and gel shift procedures. By Western blot, this antibody detects a 58 kDa and 60 kDa protein representing VDR in avians while the VDRs of mammalian species appear as single bands within the 52-55 kDa range. The MA1-710 immunogen is partially purified chicken intestinal cytoplasmic 1,25-(OH)2D3 receptor protein. This antibody recognizes an epitope between amino acid residues 89 and 105 of human VDR. This region is just C-terminal to the DNA binding domain of the VDR.

Steroid receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate hormone. The 1,25-dihydroxy-vitamin D3 receptor (VDR) belongs to the superfamily of steroid hormone receptors which includes estrogen, progesterone, glucocorticoid, androgen, and thyroid hormone receptors. Vitamin D modulates calcium and phosphorus homeostasis, bone remodeling, cell growth regulation, and differentiation. Studies have found VDR in the intestine, bone, kidney, epidermis, and cells of the endocrine immune system. Repression of T-cell proliferation and interleukin-2 (IL-2) gene expression, for example, occurs when VDR binds within the IL-2 enhancer. Formation of VDR/retinoic X receptor (RXR) heterodimers in the presence of intracellular 1,25(OH)2D3 has been shown to interfere with assembly of nuclear factor of activated T-cells (NFATp)/Fos/Jun/DNA complex and subsequent IL-2 gene transcription. The corresponding gene for the vitamin D receptor is NR1I1.