Cell Signaling Technology

Product Pathways - Translational Control

DDX5 Antibody #4387

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk Endogenous 70 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

DDX5 Antibody detects endogenous levels of total DDX5 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly487 of human DDX5. Antibodies are purified by protein A and peptide affinity chromatography.

Western blot analysis of extracts from various cell lines using DDX5 Antibody.

Background

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).

  1. Ford, M.J. et al. (1988) Nature 332, 736-8.
  2. Hirling, H. et al. (1989) Nature 339, 562-4.
  3. Fukuda, T. et al. (2007) Nat Cell Biol 9, 604-11.
  4. Davis, B.N. et al. (2008) Nature 454, 56-61.
  5. Camats, M. et al. (2008) PLoS ONE 3, e2926.
  6. Wilson, B.J. et al. (2004) BMC Mol Biol 5, 11.
  7. Jensen, E.D. et al. (2008) J Cell Biochem 103, 1438-51.
  8. Bates, G.J. et al. (2005) EMBO J 24, 543-53.
  9. Warner, D.R. et al. (2004) Biochem Biophys Res Commun 324, 70-6.
  10. Rossow, K.L. and Janknecht, R. (2003) Oncogene 22, 151-6.
  11. Yang, L. et al. (2006) Cell 127, 139-55.
  12. Yang, L. et al. (2007) J Biol Chem 282, 16811-9.
  13. Carter, C.L. et al. (2010) Oncogene 29, 5427-36.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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