Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

Pontin/RUVBL1 Antibody #12300

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Hm Mk Endogenous 50 kDa Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster  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

Pontin/RUVBL1 Antibody recognizes endogenous levels of total Pontin/RUVBL1 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human Pontin/RUVBL1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Pontin/RUVBL1 Antibody.

Background

Reptin/RuvBL2 and Pontin/RuvBL1 are closely related members of the AAA+ (ATPase Associated with diverse cellular Activities) superfamily of proteins, and are putatively homologous to bacterial RuvB proteins that drive branch migration of Holliday junctions (1). Reptin and Pontin function together as essential components of chromatin remodeling and modification complexes, such as INO80, TIP60, SRCAP, and Uri1, which play key roles in regulating gene transcription (1,2). In their capacity as essential transcriptional co-regulators, Reptin and Pontin have both been implicated in oncogenic transformations, including those driven by c-Myc, β-catenin, and E1A (2-7).

A number of research studies have reported elevated levels of Pontin in selected cancer subtypes, including hepatocellular carcinoma and colon cancer (8-10). Interestingly, Pontin was reported to potentiate the TCF/LEF1-β-catenin transcriptional complex, whereas Reptin was antagonistic to the same complex, highlighting their related, but non-redundant, function (5). Research studies also suggest a functional role for Pontin and Reptin in the DNA damage response. Both proteins are phosphorylated by ATM and Rad3-related following DNA damage (11), while Pontin is reportedly required for TIP60 activity during the DNA damage response (12).

  1. Jha, S. and Dutta, A. (2009) Mol Cell 34, 521-33.
  2. Gallant, P. (2007) Trends Cell Biol 17, 187-92.
  3. Huber, O. et al. (2008) Cancer Res 68, 6873-6.
  4. Kim, J.H. et al. (2005) Nature 434, 921-6.
  5. Bauer, A. et al. (2000) EMBO J 19, 6121-30.
  6. Wood, M.A. et al. (2000) Mol Cell 5, 321-30.
  7. Dugan, K.A. et al. (2002) Oncogene 21, 5835-43.
  8. Blanc, J.F. et al. (2005) Proteomics 5, 3778-89.
  9. Lauscher, J.C. et al. (2007) Hum Pathol 38, 978-85.
  10. Huber, O. et al. (2008) Cancer Res 68, 6873-6.
  11. Matsuoka, S. et al. (2007) Science 316, 1160-6.
  12. Jha, S. et al. (2008) Mol Cell Biol 28, 2690-700.

Application References

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Companion Products

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

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