|Other Names||Zinc finger MIZ domain-containing protein 1, PIAS-like protein Zimp10, Retinoic acid-induced protein 17, ZMIZ1, KIAA1224, RAI17, ZIMP10|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6236a was selected from the C-term region of human RAI17 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||KIAA1224, RAI17, ZIMP10|
|Function||Increases ligand-dependent transcriptional activity of AR and promotes AR sumoylation. The stimulation of AR activity is dependent upon sumoylation.|
|Cellular Location||Nucleus speckle. Cytoplasm|
|Tissue Location||Expressed most abundantly in ovary and, at lower levels, in prostate, spleen and testis. Weak expression, if any, in thymus, small intestine, colon and peripheral blood leukocytes.|
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Retinoic acid plays a critical role in development, cellular growth, and differentiation and induces the expression of a variety of genes. RAI17 expression is induced by retinoic acid and is predominantly expressed in heart, brain and ovaries. Within brain, highest expression is in amygdala. The deduced 1,067-amino acid protein contains an MSX-interacting zinc finger (MIZ) domain, a nuclear localization signal sequence, and 2 proline-rich regions. A strong intrinsic transactivation domain is identified in the C-terminal proline-rich region. RAI17 expression is detected in various cancer cell lines. RAI17 colocalizes with endogenous androgen receptor (AR) in the nuclei of prostate epithelial cells from human tissue samples. In human prostate cancer cells, RAI17 increases the transcriptional activity of AR. Studies using sumoylation-deficient AR mutants suggest that the increase of AR activity by RAI17 is dependent upon receptor sumoylation.
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