货号 | 75336S |
同种亚型 | Rabbit IgG |
反应种属 | Human\Mouse\Rat |
来源宿主 | Rabbit IgG |
应用 | WB, IP , ChIP |
目标/特异性 | Acetyl-Histone H2AZ (Lys4/Lys7) recognizes endogenous levels of histone H2AZ protein only when acetylated at Lys4 and/or Lys7. This antibody does not cross-react with other acetylated histones, including histone H2A acetylated at Lys5. This antibody also detects a band around 22 kDa, which is most likely monoubiquitylated histone H2AZ that is acetylated on Lys4 and Lys7. |
使用方法 | W IP ChIP |
供应商 | CST |
灵敏度 | Endogenous |
背景 | Modulation of chromatin structure plays a critical role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). There are five major variants of histone H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and H2A.Z (2). Histone H2A.Z, the most conserved variant across species, functions as both a positive and negative regulator of transcription and is important for chromosome stability (2). Several homologous protein complexes, such as SWR-C (S. cerevisiae), TIP60 (D. melanogaster) and SRCAP (mammals), have been shown to catalyze the ATP-dependent exchange of H2A.Z for H2A in the nucleosome (3,4,5). This exchange of histone H2A variants changes histone-histone interactions in the nucleosome core and alters an acidic patch on the surface of the nucleosome, resulting in changes in nucleosome stability and binding of non-histone proteins such as HP1α (6,7). Acetylation of Histone H2AZ correlates with gene activity (8). Acetylation of Histone H2AZ on Lys4 and Lys7 occurs at the 5 end of genes and confers nucleome destabilization and open chromatin confirmation required for tanscriptional activation (9-11). |
存放说明 | -20C |
计算分子量 | 14 |
参考文献 | 1 . Jin, J. et al. (2005) Trends Biochem Sci 30, 680-7. 2 . Raisner, R.M. and Madhani, H.D. (2006) Curr Opin Genet Dev 16, 119-24. 3 . Mizuguchi, G. et al. (2004) Science 303, 343-8. 4 . Kusch, T. et al. (2004) Science 306, 2084-7. 5 . Ruhl, D.D. et al. (2006) Biochemistry 45, 5671-7. 6 . Suto, R.K. et al. (2000) Nat Struct Biol 7, 1121-4. 7 . Fan, J.Y. et al. (2004) Mol Cell 16, 655-61. 8 . Millar, C.B. et al. (2006) Genes Dev 20, 711-22. 9 . Bruce, K. et al. (2005) Nucleic Acids Res 33, 5633-9. 10 . Ishibashi, T. et al. (2009) Biochemistry 48, 5007-17. 11 . Valdés-Mora, F. et al. (2012) Genome Res 22, 307-21. |
Chromatin immunoprecipitations were performed with cross-linked chromatin from 4 x 106 LNCaP cells treated with Trichostatin A (TSA) #9950 (100 nM, 24 hr) and either 10 μl of Acetyl-Histone H2AZ (Lys4/7) (D3V1I) Rabbit mAb or 2 μl of Normal Rabbit IgG #2729 using SimpleChIP® Enzymatic Chromatin IP Kit (Magnetic Beads) #9003. The enriched DNA was quantified by Real-Time PCR using human CAV1 promoter primers, SimpleChIP® Human KLK2 Intron 1 Primers #62086, and SimpleChIP® Human α Satelite Repeat Primers #4486. The amount of immunoprecipitated DNA in each sample is represented as signal relative to the total amount of input chromatin, which is equivalent to one. | |
Western blot analysis of extracts from HeLa cells, untreated (-) or treated (+) with Trichostatin A (TSA) #9950 (1 μM, 18 hr), using Acetyl-Histone H2AZ (Lys4/Lys7) Rabbit mAb (upper) or Histone H2AZ Antibody #2718 (lower). |