Revision 1

#8340Store at -20C

1 个试剂盒

(7 x 20 microliters)

Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

Support: 877-678-TECH (8324)

Web: [email protected] cellsignal.com

3 Trask LaneDanversMassachusetts01923USA
For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
JARID1A (D28B10) Rabbit mAb 3876 20 µl 200 kDa Rabbit IgG
JARID1B Antibody 3273 20 µl 180 kDa Rabbit 
JARID1C (D29B9) Rabbit mAb 5361 20 µl 180 kDa Rabbit IgG
JMJD2A (C37E5) Rabbit mAb 5328 20 µl 150 kDa Rabbit IgG
JMJD1B (6A1-1F5) Mouse mAb 5377 20 µl 220 kDa Mouse IgG1
JMJD2B (D7E6) Rabbit mAb 8639 20 µl 150 kDa Rabbit IgG
PHF2 (D45A2) Rabbit mAb 3497 20 µl 150 kDa Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl Horse 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

Description

The Jumonji Family Antibody Sampler Kit provides an economical means of evaluating total levels of Jumonji family proteins. The kit contains enough primary antibodies to perform two western blot experiments with each primary antibody.

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.

Background

Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (1). 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 (1). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into 7 separate families (1).

The JMJD2 (Jumonji domain-containing protein 2) family, also known as JHDM3 (JmjC domain-containing histone demethylation protein 3) family, contains four members: JMJD2A/JHDM3A, JMJD2B/JHDM3B, JMJD2C/JHDM3C, and JMJD2D/JHDM3D. In addition to the JmjC domain, these proteins also contain JmjN, PHD and Tudor domains, the latter of which has been shown to bind to methylated histone H3 at Lys4 and Lys9, and methylated histone H4 at Lys20 (2,3). JMJD2 proteins have been shown to demethylate di- and tri-methyl histone H3 at Lys9 and Lys36, and function as both activators and repressors of transcription (4-9). JMJD2A, JMJD2C and JMJD2D function as coactivators of the androgen receptor in prostate tumor cells (5). In contrast, JMJD2A also associates with Rb and N-CoR corepressor complexes and is necessary for transcriptional repression of target genes (6,7). JMJD2B antagonizes histone H3 Lys9 tri-methylation at pericentric heterochromatin (8). JMJD1B is a more widely expressed family member and is frequently deleted in myeloid leukemia (10).

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) (11). 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) (11). All four JARID proteins demethylate di- and tri-methyl histone H3 Lys4; JARID1B also demethylates mono-methyl histone H3 Lys4 (12-14). JARID1A is a critical RB-interacting protein and is required for Polycomb-Repressive Complex 2 (PRC2)-mediated transcriptional repression during ES cell differentiation (15). A JARID1A-NUP98 gene fusion is associated with myeloid leukemia (16). JARID1B, which interacts with many proteins including c-Myc and HDAC4, may play a role in cell fate decisions by blocking terminal differentiation (17-19). JARID1B is over-expressed in many breast cancers and may act by repressing multiple tumor suppressor genes including BRCA1 and HOXA5 (20,21). 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 (14). JARID1D is largely uncharacterized. PHF2 contains a JmjC domain, which may play a role in histone demethylation (1).

  1. Klose, R.J. et al. (2006) Nat Rev Genet 7, 715-27.
  2. Chen, Z. et al. (2007) Proc Natl Acad Sci U S A 104, 10818-23.
  3. Lee, J. et al. (2008) Nat Struct Mol Biol 15, 109-11.
  4. Whetstine, J.R. et al. (2006) Cell 125, 467-81.
  5. Shin, S. and Janknecht, R. (2007) Biochem Biophys Res Commun 359, 742-6.
  6. Gray, S.G. et al. (2005) J Biol Chem 280, 28507-18.
  7. Zhang, D. et al. (2005) Mol Cell Biol 25, 6404-14.
  8. Fodor, B.D. et al. (2006) Genes Dev 20, 1557-62.
  9. Cloos, P.A. et al. (2006) Nature 442, 307-11.
  10. Hu, Z. et al. (2001) Oncogene 20, 6946-54.
  11. Benevolenskaya, E.V. (2007) Biochem Cell Biol 85, 435-43.
  12. Christensen, J. et al. (2007) Cell 128, 1063-76.
  13. Yamane, K. et al. (2007) Mol Cell 25, 801-12.
  14. Tahiliani, M. et al. (2007) Nature 447, 601-5.
  15. Pasini, D. et al. (2008) Genes Dev 22, 1345-55.
  16. van Zutven, L.J. et al. (2006) Genes Chromosomes Cancer 45, 437-46.
  17. Secombe, J. et al. (2007) Genes Dev 21, 537-51.
  18. Barrett, A. et al. (2007) Int J Cancer 121, 265-75.
  19. Dey, B.K. et al. (2008) Mol Cell Biol 28, 5312-27.
  20. Barrett, A. et al. (2002) Int J Cancer 101, 581-8.
  21. Lu, P.J. et al. (1999) J Biol Chem 274, 15633-45.

Background References

    Trademarks and Patents

    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
    All other trademarks are the property of their respective owners. Visit cellsignal.com/trademarks for more information.

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