Anti-Vitamine D Receptor/VDR Antibody Picoband® 31.0550 Vervoeging

VDR (Vitamin D Receptor), also known as Vitamin D Hormone Receptor, is a member of the nuclear receptor family of transcription factors. Labuda et al. (1991) assigned the VDR gene to 12q12-q14 by in situ hybridization. Using mutation analysis, Jurutka et al. (2000) characterized arg18/arg22, VDR residues immediately N-terminal of the first DNA-binding zinc finger, as vital for contact with the general transcription factor IIB (TFIIB) . A natural polymorphic variant of VDR, termed F/M4 (missing a FokI restriction site), which lacks only the first 3 amino acids (including glu2), interacted more efficiently with TFIIB and also possessed elevated transcriptional activity compared with the full-length (f/M1) receptor. Shah et al. (2006) stated that the signaling and oncogenic activity of beta-catenin (CTNNB1) can be repressed by activation of VDR. Conversely, high levels of beta-catenin can potentiate the transcriptional activity of 1,25- dihydroxyvitamin D3.

GTP-binding nuclear protein Ran; Androgen receptor-associated protein 24; GTPase Ran; Ras-like protein TC4; Ras-related nuclear protein; RAN; ARA24; OK/SW-cl.81

VDR

7421

P11473

Human, Mouse, Rat

No cross-reactivity with other proteins.

A synthetic peptide corresponding to a sequence at the C-terminus of human Vitamin D Receptor/VDR, which shares 88.9% amino acid (aa) sequence identity with mouse and rat VDR.

Expressed in a variety of tissues. .

Flow Cytometry

Small G Proteins, Spindle

Immunogen affinity purified.

Liquid

GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity) . The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. .

1. Jurutka, P. W., Remus, L. S., Whitfield, G. K., Thompson, P. D., Hsieh, J.-C., Zitzer, H., Tavakkoli, P., Galligan, M. A., Dang, H. T. L., Haussler, C. A., Haussler, M. R. The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB. Molec. Endocr. 14: 401-420, 2000. 2. Labuda, M., Ross, M. V., Fujiwara, T. M., Morgan, K., Ledbetter, D., Hughes, M. R., Glorieux, F. H. Two hereditary defects related to vitamin D metabolism map to the same region of human chromosome 12q.II (Abstract) Cytogenet. Cell Genet. 58: 1978, 1991. 3. Shah, S., Islam, M. N., Dakshanamurthy, S., Rizvi, I., Rao, M., Herrell, R., Zinser, G., Valrance, M., Aranda, A., Moras, D., Norman, A., Welsh, J., Byers, S. W. The molecular basis of vitamin D receptor and beta-catenin crossregulation. Molec. Cell 21: 799-809, 2006. Note: Erratum: Molec. Cell 21: 148 only, 2006.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

24423 MW

6

GTP-binding nuclear protein Ran

Nucleus. Cytoplasm. Melanosome. Nucleus envelope . Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis. Colocalizes with NEMP1 at the nuclear envelope (By similarity) . Identified by mass spectrometry in melanosome fractions from stage I to stage IV. .

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.