|Other Names||Ran-binding protein 9, RanBP9, BPM-L, BPM90, Ran-binding protein M, RanBPM, RanBP7, RANBP9, RANBPM|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8501c was selected from the Center region of human RANBP9. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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.|
|Function||May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity).|
|Cellular Location||Cytoplasm, cytosol. Nucleus. Note==Predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane|
|Tissue Location||Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells.|
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Provided below are standard protocols that you may find useful for product applications.
RANBP9 is a protein that binds RAN, a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The protein has also been shown to interact with several other proteins, including met proto-oncogene, homeodomain interacting protein kinase 2, androgen receptor, and cyclin-dependent kinase 11.
Caballero,O.L., et.al., Oncogene 21 (19), 3003-3010 (2002)
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