Product Pathways - Chromatin Regulation / Epigenetics
Phospho-DBC1 (Thr454) Antibody #4880
|W IP IF-IC||H||Endogenous||130||Rabbit|
Reactivity Key: H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-DBC1 (Thr454) Antibody detects endogenous levels of DBC1 only when phosphorylated on Thr454.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to Thr454 of the human DBC1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from 293 and HeLa cell lines, untreated or UV-treated (100 J/m2 and 4 hour recovery), using Phospho-DBC1 (Thr454) Antibody (upper) or β-actin Antibody #4967 (lower).
Deleted in breast cancer gene 1 protein (DBC1) was originally identified by its localization to a region of chromosome 8p21 that is homozygously deleted in breast cancer (1). DBC1 is a large, nuclear protein with multiple functions in cell survival. It binds directly to the estrogen receptor α (ERα) hormone-binding domain in a ligand-independent manner and may be a key determinant of ligand-independent ERα expression and survival in human breast cancer cells (2). DBC1 can promote p53-mediated apoptosis by binding to and inhibiting the deacetylase activity of SirT1, resulting in increased p53 acetylation levels and activity (3). DBC1 may be an important regulator of heterochromatin formation as it binds SUV39H1 and inhibits its histone methyltransferase activity (4). Caspase-dependent processing activates the pro-apoptotic activity of DBC1 during Tumor Necrosis Factor-α (TNF-α)-mediated cell death signaling (5). This processing of DBC1 in response to TNF-α is an early event in the onset of apoptosis and results in relocalization of DBC1 to the cytoplasm. Overexpression of the processed, cytoplasmic form of DBC1 results in mitochondrial clustering and matrix condensation and sensitizes cells to TNF-α-mediated apoptosis.
The threonine residue at 454 of DBC1 is phosphorylated in an ATM/ATR-dependent manner in response to DNA damage (6,7). Phospho-DBC1 (Thr454) Antibody is directed at a site that was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for modification site discovery. Phosphorylation at Thr454 was discovered using an ATM/ATR substrate antibody and was shown to be induced by UV treatment. Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information.
- Hamaguchi, M. et al. (2002) Proc Natl Acad Sci USA 99, 13647-52.
- Trauernicht, A.M. et al. (2007) Mol Endocrinol 21, 1526-36.
- Zhao, W. et al. (2008) Nature 451, 587-90.
- Li, Z. et al. (2009) J Biol Chem 284, 10361-6.
- Sundararajan, R. et al. (2005) Oncogene 24, 4908-20.
- Stokes, M.P. et al. (2007) Proc Natl Acad Sci USA 104, 19855-60.
- Beausoleil, S.A. et al. (2004) Proc Natl Acad Sci USA 101, 12130-5.
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For Research Use Only. Not For Use In Diagnostic Procedures.