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  3. BRD Antibody Sampler Kit

BRD Antibody Sampler Kit #26642

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    Kit Usage Information

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    Product Description

    The BRD Antibody Sampler Kit provides an economical means of detecting various BRD family members using antibodies. The kit contains enough antibodies to perform two western blot experiments with each primary antibody.

    Background

    Bromodomain-containing protein 1 (BRD1), BRD2, BRD3, BRD4, and BRDT are members of the bromodomain and extra terminal (BET) family of proteins (1-3). BET family proteins contain two tandem bromodomains and an extra terminal (ET) domain, and bind acetyl lysine residues (3). BRD1 is part of a histone acetyltransferase complex with HBO1 and is responsible for global acetylation of Lys14 on histone H3 (4). BRD1 contains a unique PHD finger domain with a positively charged surface that binds DNA via interactions with histone H3 (5,6). By driving histone acetylation around key genes, BRD1 has been implicated in many cellular functions, including stem cell differentiation, T cell development, and erythropoiesis (4,7,8). The BRD1 gene has been shown to confer susceptibility to schizophrenia and bipolar disorder (9,10). BRD1 overexpression has been described in colorectal cancer, and BRD1 inhibition has been shown to increase immune therapy efficacy in high-grade ovarian cancer (11,12). BRD2 is involved in expression of cell cycle genes by binding to E2Fs (13).

    BRD2 is associated with many transcription regulators, including TFIID and Swi/Snf complexes (14,15). Like other bromodomain proteins, BRD2 is thought to function in mammalian development by regulating chromatin structure and transcription (14,16). BRD2 binds acetylated histone H4 Lys12, a substrate of several histone acetyltransferase transcriptional coactivators (17). In mouse, BRD2 has the highest levels of expression during embryogenesis and in the adult testis, ovaries, and brain (14,18,19). BRD2-deficient mouse embryos exhibit delayed development and death due to neural tube closure defects (16). Mutations in BRD2 have been associated with susceptibility to juvenile myoclonic epilepsy (JME) (20).

    BRD3 binds acetylated Lys14 on histone H3, and Lys5 and Lys12 on histone H4 to promote transcription (21). BRD3 plays a role in erythroid development by binding to GATA1, facilitating its binding to target genes (22). The BRD3 gene can be fused to nuclear protein in testis (NUT) in NUT midline carcinomas (23).

    BRD4 binds acetylated Lys14 on histone H3, and Lys5 and Lys12 on histone H4 (24). BRD4 binding occurs throughout the cell cycle, including during mitosis when many genes are silenced (25). BRD4 accelerates reactivation of silenced genes upon exit from mitosis (2,26). BRD4 facilitates transcription by recruiting the pTEFb complex, which phosphorylates Ser2 of the C-terminal domain of RNA polymerase II, thereby promoting transcription elongation (3,27,28). BRD4 is part of the super elongation complex and the polymerase-associated factor complex (PAFc) in MLL-fusion derived leukemia cell lines, demonstrating a role for BRD4 in the regulation of transcription elongation (29). BRD4 is a promising therapeutic target for various Myc-driven cancers, such as Burkitt’s lymphoma and certain acute myeloid leukemias (1,30,31). BRD4 regulates the expression of inflammatory genes, and inhibition of BRD4 (and BET family proteins) chromatin binding causes reduced expression of a subset of inflammatory genes in macrophages, leading to protection against endotoxic shock and sepsis (32).

    BRDT is expressed in the testes and is essential for male germ cell differentiation, acting as a master regulator of meiotic divisions and post-meiotic genome repackaging (33,34). JQ1 treatment of BRDT has been explored as a potential male contraceptive, as JQ1-treated mice exhibit reduced spermatozoa number and motility without affecting hormone levels (35). Inhibition of BET proteins induces apoptosis in various MLL-fusion driven leukemic cell lines by competing BRD3 and BRD4 from chromatin, reducing expression of BCL2, Myc, and CDK6 (29). BET inhibition has antitumor activities against NUT midline carcinoma cell lines and xenografts in mice, where BRD4 is found to be a frequent translocation partner of the NUT protein (36).
    1. Belkina, A.C. and Denis, G.V. (2012) Nat Rev Cancer 12, 465-77.
    2. Voigt, P. and Reinberg, D. (2011) Genome Biol 12, 133.
    3. Wu, S.Y. and Chiang, C.M. (2007) J Biol Chem 282, 13141-5.
    4. Mishima, Y. et al. (2011) Blood 118, 2443-53.
    5. Liu, L. et al. (2012) J Struct Biol 180, 165-73.
    6. Qin, S. et al. (2011) J Biol Chem 286, 36944-55.
    7. Cho, H.I. et al. (2016) Exp Cell Res 346, 30-9.
    8. Mishima, Y. et al. (2014) Nat Commun 5, 5872.
    9. Severinsen, J.E. et al. (2006) Mol Psychiatry 11, 1126-38.
    10. Nyegaard, M. et al. (2010) Am J Med Genet B Neuropsychiatr Genet 153B, 582-591.
    11. Li, Z. et al. (2021) Technol Cancer Res Treat 20, 15330338211039678.
    12. Wan, C. et al. (2021) Cancer Res 81, 158-173.
    13. Denis, G.V. et al. (2000) Cell Growth Differ 11, 417-24.
    14. Crowley, T.E. et al. (2002) Mol Endocrinol 16, 1727-37.
    15. Denis, G.V. et al. (2006) J Proteome Res 5, 502-11.
    16. Gyuris, A. et al. (2009) Biochim Biophys Acta 1789, 413-21.
    17. Kanno, T. et al. (2004) Mol Cell 13, 33-43.
    18. Shang, E. et al. (2004) Gene Expr Patterns 4, 513-9.
    19. Trousdale, R.K. and Wolgemuth, D.J. (2004) Mol Reprod Dev 68, 261-8.
    20. Pal, D.K. et al. (2003) Am J Hum Genet 73, 261-70.
    21. LeRoy, G. et al. (2008) Mol Cell 30, 51-60.
    22. Lamonica, J.M. et al. (2011) Proc Natl Acad Sci USA 108, E159-68.
    23. French, C.A. et al. (2008) Oncogene 27, 2237-42.
    24. Dey, A. et al. (2003) Proc Natl Acad Sci USA 100, 8758-63.
    25. Dey, A. et al. (2009) Mol Biol Cell 20, 4899-909.
    26. Zhao, R. et al. (2011) Nat Cell Biol 13, 1295-304.
    27. Jang, M.K. et al. (2005) Mol Cell 19, 523-34.
    28. Yang, Z. et al. (2005) Mol Cell 19, 535-45.
    29. Dawson, M.A. et al. (2011) Nature 478, 529-33.
    30. Muller, S. et al. (2011) Expert Rev Mol Med 13, e29.
    31. Mertz, J.A. et al. (2011) Proc Natl Acad Sci USA 108, 16669-74.
    32. Nicodeme, E. et al. (2010) Nature 468, 1119-23.
    33. Shang, E. et al. (2007) Development 134, 3507-15.
    34. Gaucher, J. et al. (2012) EMBO J 31, 3809-20.
    35. Matzuk, M.M. et al. (2012) Cell 150, 673-84.
    36. Filippakopoulos, P. et al. (2010) Nature 468, 1067-73.

    Database Links

    UniProt ID: P25440 , O60885 , Q58F21 , Q15059 , O95696


    Entrez-Gene Id: 6046 , 23476 , 676 , 8019 , 23774


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