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Product Usage Information

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 μg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

JARID1A (D28B10) Rabbit mAb detects endogenous levels of total JARID1A protein (both isoforms). The antibody does not cross-react with other JARID proteins, including JARID1B, JARID1C and JARID1D.

Species Reactivity:

Human, Mouse

Species predicted to react based on 100% sequence homology:

Rat, Bovine

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the human JARID1A protein.

Background

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 overexpressed 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 uniquely localized to the Y chromosome, and functions as a tumor suppressor by repressing genes associated with cell invasiveness (17). JARID1D is frequently mutated in metastatic prostate tumors, and low JARID1D levels are associated with poor prognosis in prostate cancer patients (17).

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.
17. Li, N. et al. (2016) Cancer Res 76, 831-43.