JARID1B Antibody

3273:

Immunoprecipitation , Western Blotting

JARID1B Antibody detects endogenous levels of JARID1B protein. The antibody does not cross-react with other JARID proteins, including JARID1A, JARID1C and JARID1D.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the human JARID1B protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from MCF-7, T-47D and COS cells using JARID1B Antibody.

The methylation state of lysine residues in histone proteins is a major determinant for formation of active and inactive regions of the genome and is crucial for proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain can catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into 7 separate families (3). The JARID (Jumonji/AT-rich interactive domain-containing protein) family contains four members: JARID1A (also RBP2 and RBBP2), JARID1B (also PLU-1), JARID1C (also SMCX) and JARID1D (also SMCY) (4). In addition to the JmJC domain, these proteins contain JmJN, BRIGHT, C5HC2 zinc-finger, and PHD domains, the latter of which binds to methylated histone H3 (Lys9) (4). All four JARID proteins demethylate di- and tri-methyl histone H3 Lys4; JARID1B also demethylates mono-methyl histone H3 Lys4 (5-7). JARID1A is a critical RB-interacting protein and is required for Polycomb-Repressive Complex 2 (PRC2)-mediated transcriptional repression during ES cell differentiation (8). A JARID1A-NUP98 gene fusion is associated with myeloid leukemia (9). JARID1B, which interacts with many proteins including c-Myc and HDAC4, may play a role in cell fate decisions by blocking terminal differentiation (10-12). JARID1B is over-expressed in many breast cancers and may act by repressing multiple tumor suppressor genes including BRCA1 and HOXA5 (13,14). JARID1C has been found in a complex with HDAC1, HDAC2, G9a and REST, which binds to and represses REST target genes in non-neuronal cells (7). JARID1C mutations are associated with X-linked mental retardation and epilepsy (15,16). JARID1D is largely uncharacterized.

1. Kubicek, S. et al. (2006) Ernst Schering Res Found Workshop , 1-27.
2. Lin, W. and Dent, S.Y. (2006) Curr Opin Genet Dev 16, 137-42.
3. Klose, R.J. et al. (2006) Nat Rev Genet 7, 715-27.
4. Benevolenskaya, E.V. (2007) Biochem Cell Biol 85, 435-43.
5. Christensen, J. et al. (2007) Cell 128, 1063-76.
6. Yamane, K. et al. (2007) Mol Cell 25, 801-12.
7. Tahiliani, M. et al. (2007) Nature 447, 601-5.
8. Pasini, D. et al. (2008) Genes Dev 22, 1345-55.
9. van Zutven, L.J. et al. (2006) Genes Chromosomes Cancer 45, 437-46.
10. Secombe, J. et al. (2007) Genes Dev 21, 537-51.
11. Barrett, A. et al. (2007) Int J Cancer 121, 265-75.
12. Dey, B.K. et al. (2008) Mol Cell Biol 28, 5312-27.
13. Barrett, A. et al. (2002) Int J Cancer 101, 581-8.
14. Lu, P.J. et al. (1999) J Biol Chem 274, 15633-45.
15. Tzschach, A. et al. (2006) Hum Mutat 27, 389.
16. Jensen, L.R. et al. (2005) Am J Hum Genet 76, 227-36.

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