Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

Brd2 (D89B4) Rabbit mAb #5848

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M (R) (Mk) Endogenous 110 Rabbit IgG

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

Brd2 (D89B4) Rabbit mAb recognizes endogenous levels of total Brd2 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala310 of human Brd2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from MOLT-4 and NCCIT cells using Brd2 (D89B4) Rabbit mAb.

Background

Brd2 is a highly conserved member of the BET subfamily of bromodomain proteins that contain two tandem N-terminal bromodomains and a single C-terminal extra-terminal (ET) domain (1). In addition to its involvement in guiding the expression of cell cycle genes through its binding to multiple E2Fs (2), Brd2 has been shown to be associated with several regulators of transcription, including TFIID and Swi/Snf complexes (3,4). First identified as a nuclear serine/threonine kinase (5), Brd2, like other bromodomain proteins, is thought to function in mammalian development by regulating chromatin structure and transcription (6). Brd2 has been shown to bind to histone H4 via acetylated Lys12, a substrate of several histone acetyltransferase transcriptional coactivators (7). In mouse, Brd2 has the highest levels of expression during embryogenesis and in the adult testis, ovaries, and brain (8,9,10). Brd2-deficient mouse embryos exhibit delayed development and eventual death due to neural tube closure defects (11). Mutations in the promoter of the Brd2 gene have been associated with increased susceptibility to juvenile myoclonic epilepsy (JME) (12).

  1. Florence, B. and Faller, D.V. (2001) Front Biosci 6, D1008-18.
  2. Denis, G.V. et al. (2000) Cell Growth Differ 11, 417-24.
  3. Crowley, T.E. et al. (2002) Mol Endocrinol 16, 1727-37.
  4. Denis, G.V. et al. (2006) J Proteome Res 5, 502-11.
  5. Denis, G.V. et al. (2000) Cell Growth Differ 11, 417-24.
  6. Gyuris, A. et al. (2009) Biochim Biophys Acta 1789, 413-21.
  7. Kanno, T. et al. (2004) Mol Cell 13, 33-43.
  8. Shang, E. et al. (2004) Gene Expr Patterns 4, 513-9.
  9. Trousdale, R.K. and Wolgemuth, D.J. (2004) Mol Reprod Dev 68, 261-8.
  10. Crowley, T.E. et al. (2002) Mol Endocrinol 16, 1727-37.
  11. Gyuris, A. et al. (2009) Biochim Biophys Acta 1789, 413-21.
  12. Pal, D.K. et al. (2003) Am J Hum Genet 73, 261-70.

Application References

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

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