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Product last modified at: 2025-01-01T09:11:32.852Z
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PDP - Template Name: Antibody Duet
PDP - Template ID: *******ad0fa02

PhosphoPlus® PBRM1/BAF180 (Ser948) Antibody Duet #38239

    Product Information

    Product Description

    PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

    Background

    ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9).

    PBRM1/BAF180 is a unique member of the SWI/SNF complex PBAF, which binds to kinetochores in mitotic chromatin (10,11). PBAF is involved in nuclear receptor-mediated transcription and retinoic acid driven gene activation (12,13). PBRM1/BAF180 has been shown to be a potent tumor suppressor, as it is the second-most mutated gene in renal carcinomas (14). Mutations of PBRM1/BAF180 have also been shown to be involved in breast cancer, and low expression relates to poorer prognosis (15,16). PBRM1/BAF180 is phosphorylated at Ser948 by ATM during DNA damage, which is important for transcriptional silencing and repair around double-stranded breaks (17).
    PBRM1/BAF180 is phosphorylated at Ser948 by ATM during DNA damage, which is important for transcriptional silencing and repair around double-stranded breaks (17).
    1. Ho, L. and Crabtree, G.R. (2010) Nature 463, 474-84.
    2. Becker, P.B. and Hörz, W. (2002) Annu Rev Biochem 71, 247-73.
    3. Eberharter, A. and Becker, P.B. (2004) J Cell Sci 117, 3707-11.
    4. Bowman, G.D. (2010) Curr Opin Struct Biol 20, 73-81.
    5. Gangaraju, V.K. and Bartholomew, B. (2007) Mutat Res 618, 3-17.
    6. Lessard, J.A. and Crabtree, G.R. (2010) Annu Rev Cell Dev Biol 26, 503-32.
    7. Morettini, S. et al. (2008) Front Biosci 13, 5522-32.
    8. Wolf, I.M. et al. (2008) J Cell Biochem 104, 1580-6.
    9. Simone, C. (2006) J Cell Physiol 207, 309-14.
    10. Nie, Z. et al. (2000) Mol Cell Biol 20, 8879-88.
    11. Xue, Y. et al. (2000) Proc Natl Acad Sci U S A 97, 13015-20.
    12. Lemon, B. et al. (2001) Nature 414, 924-8.
    13. Wang, Z. et al. (2004) Genes Dev 18, 3106-16.
    14. Varela, I. et al. (2011) Nature 469, 539-42.
    15. Xia, W. et al. (2008) Cancer Res 68, 1667-74.
    16. Mo, D. et al. (2015) Int J Clin Exp Pathol 8, 9307-13.
    17. Kakarougkas, A. et al. (2014) Mol Cell 55, 723-32.
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