Product Pathways - Chromatin Regulation / Epigenetics
Reptin/RuvBL2 (D8N3J) Rabbit mAb #12668
|12668S||100 µl (10 western blots)||---||In Stock||---|
|12668||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||48||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Hamster, Xenopus, Zebrafish, Bovine, Dog, Pig, Guinea Pig.
Specificity / Sensitivity
Reptin/RuvBL2 (D8N3J) Rabbit mAb recognizes endogenous levels of total Reptin/RuvBL2 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly263 of human Reptin/RuvBL2 protein.
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).
Reptin plays a role in modulating cellular responses to hypoxia. Hypoxia induced methylation of Reptin by the methyltransferase G9a leads to its recruitment to hypoxia responsive promoters, where it negatively regulates transcription of these genes (8). In addition to transcriptional regulatory roles, Reptin also participates in the telomerase biogenesis processes as part of the telomerase complex. Reptin is involved in DNA damage response as part of the TIP60 acetyltransferase complex that stimulates ATM kinase activity necessary for phosphorylation of proteins involved in both checkpoint activation and DNA repair (9,10).
- Jha, S. and Dutta, A. (2009) Mol Cell 34, 521-33.
- Gallant, P. (2007) Trends Cell Biol 17, 187-92.
- Huber, O. et al. (2008) Cancer Res 68, 6873-6.
- Kim, J.H. et al. (2005) Nature 434, 921-6.
- Bauer, A. et al. (2000) EMBO J 19, 6121-30.
- Wood, M.A. et al. (2000) Mol Cell 5, 321-30.
- Dugan, K.A. et al. (2002) Oncogene 21, 5835-43.
- Lee, J.S. et al. (2010) Mol Cell 39, 71-85.
- Venteicher, A.S. et al. (2008) Cell 132, 945-57.
- Sun, Y. et al. (2010) Cell Cycle 9, 930-6.
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