Product Pathways - Cytoskeletal Signaling
Phospho-RanBP3 (Ser58) Antibody #9380
|9380S||100 µl (10 western blots)||---||In Stock||---|
|9380||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
Phospho-RanBP3 (Ser58) Antibody recognizes endogenous levels of RanBP3b protein only when phosphorylated at Ser58, and RanBP3a protein only when phosphorylated at corresponding residue Ser126.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser58 of human RanBP3b protein. Antibodies are purified by protein A and peptide affinity chromatography.
RanBP3 was originally identified as RanGTP binding protein located in the nucleus and involved in the nuclear exporting process (1). It functions as a cofactor for CRM1 nuclear export by binding to CRM1, stabilizing the RanGTP-CRM1-cargo interaction and promoting complex association with nuclear pore proteins (2,3). In the absence of Ran-bound GTP, RanBP3 prevents binding of CRM1 complex to the nuclear pore complex. In addition to CRM1, RanBP3 also has been shown to bind to RanGEF-RCC1 and increase the guanine nucleotide exchange activity of RCC1 for RanGTP-CRM1-Cargo (1,4). In some cases, as with β-catenin and Smad2/3, RanBP3 binding may mediate the target protein nuclear export in a Ran-dependent, but CRM1-independent manner (5,6). RanBP3 is phosphorylated at Ser58 through the PI3K/Akt or ERK/RSK pathway. This phosphorylation is important for RanBP3 function in nuclear export, likely due to stimulation of RCC1 activity (7,8).
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- Lindsay, M.E. et al. (2001) J Cell Biol 153, 1391-402.
- Englmeier, L. et al. (2001) EMBO Rep 2, 926-32.
- Nemergut, M.E. et al. (2002) J Biol Chem 277, 17385-8.
- Hendriksen, J. et al. (2005) J Cell Biol 171, 785-97.
- Dai, F. et al. (2009) Dev Cell 16, 345-57.
- Yoon, S.O. et al. (2008) Mol Cell 29, 362-75.
- von Knethen, A. et al. (2010) J Cell Sci 123, 192-201.
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