Product Pathways - Protein Translation
DDX5 (D15E10) XP® Rabbit mAb #9877
|9877S||100 µl (10 western blots)||---||In Stock||---|
|9877P||40 µl (4 western blots)||---||In Stock||---|
|9877||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||68||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, IF-IC=Immunofluorescence (Immunocytochemistry)
Species predicted to react based on 100% sequence homology: Bovine, Horse.
Specificity / Sensitivity
DDX5 (D15E10) XP® Rabbit mAb recognizes endogenous levels of total DDX5 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser498 of human DDX5 protein.
Western blot analysis of extracts from various cell lines using DDX5 (D15E10) XP® Rabbit mAb.
DDX5 (DEAD box polypeptide 5), also known as p68, was first identified as a 68 kDa nuclear protein with similarity to translation initiation factor eIF-4A (1). DDX5 is a member of the DEAD box family of putative RNA helicases, defined by the presence of a conserved DEAD (Asp-Glu-Ala-Asp) motif that appears to function primarily in the regulation of RNA secondary structure. DDX5 exhibits ATP-dependent RNA helicase activity (2) and has been identified as a critical subunit of the DROSHA complex that regulates miRNA and rRNA processing (3,4). DDX may also regulate mRNA splicing (5) and has been shown to interact with HDAC1, where it can regulate promoter-specific transcription (6). DDX5 interacts with a diverse group of proteins, including Runx2, p53, Smad3, CBP, and p300 (7-10), suggesting an important role for DDX5 in a multitude of developmental processes. Notably, DDX5 may be involved in growth factor-induced epithelial mesechymal transition (EMT). Phosphorylation of DDX5 at Tyr593 following PDGF stimulation was shown to displace Axin from β-catenin; this prevented phosphorylation of β-catenin by GSK-3β, leading to Wnt-independent nuclear translocation of β-catenin (11) and increased transcription of c-Myc, cyclin D1, and Snai1 (12,13).
- Ford, M.J. et al. (1988) Nature 332, 736-8.
- Hirling, H. et al. (1989) Nature 339, 562-4.
- Fukuda, T. et al. (2007) Nat Cell Biol 9, 604-11.
- Davis, B.N. et al. (2008) Nature 454, 56-61.
- Camats, M. et al. (2008) PLoS ONE 3, e2926.
- Wilson, B.J. et al. (2004) BMC Mol Biol 5, 11.
- Jensen, E.D. et al. (2008) J Cell Biochem 103, 1438-51.
- Bates, G.J. et al. (2005) EMBO J 24, 543-53.
- Warner, D.R. et al. (2004) Biochem Biophys Res Commun 324, 70-6.
- Rossow, K.L. and Janknecht, R. (2003) Oncogene 22, 151-6.
- Yang, L. et al. (2006) Cell 127, 139-55.
- Yang, L. et al. (2007) J Biol Chem 282, 16811-9.
- Carter, C.L. et al. (2010) Oncogene 29, 5427-36.
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For Research Use Only. Not For Use In Diagnostic Procedures.
XP® is a trademark of Cell Signaling Technology, Inc.
DRAQ5® is a registered trademark of Biostatus Limited.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.