Ubiquityl-Histone H2A.Z (Lys120) (E6G7X) Rabbit mAb #68135
- WB
- ChIP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 23 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Chromatin IP | 1:50 |
| Chromatin IP-seq | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
H2A.Z is a histone H2A variant protein that is critical for proper regulation of gene expression. H2A.Z is localized throughout the genome, but appears to be most concentrated at the promoters and enhancers of active genes (8). Acetylation of histone H2A.Z at promoters and enhancers confers nucleosome destabilization and open chromatin confirmation, facilitating transcriptional activation (9-11). While the bulk of histone H2A.Z appears to be excluded from constitutive heterochromatin, histone H2A.Z is found in various forms of facultative heterochromatin, including the inactive X chromosome and transcriptionally poised bivalent gene promoters (8,12). In these heterochromatic regions of the genome, H2A.Z is mono-ubiquitylated on Lys120 and Lys121 by the Ring1B ubiquitin ligase found in the Polycomb Repressor Complex 1 (PRC1) (8,12). Mono-methylation of H2A.Z on Lys120 and Lys121 facilitates repression of gene expression by inhibiting the binding of the activating BRD4 protein and facilitating the recruitment of the Polycomb Repressor Complex 2 (PRC2), the latter of which methylates histone H3 on Lys27 and facilitates transcriptional repression (8).
- Jin, J. et al. (2005) Trends Biochem Sci 30, 680-7.
- Raisner, R.M. and Madhani, H.D. (2006) Curr Opin Genet Dev 16, 119-24.
- Mizuguchi, G. et al. (2004) Science 303, 343-8.
- Kusch, T. et al. (2004) Science 306, 2084-7.
- Ruhl, D.D. et al. (2006) Biochemistry 45, 5671-7.
- Suto, R.K. et al. (2000) Nat Struct Biol 7, 1121-4.
- Fan, J.Y. et al. (2004) Mol Cell 16, 655-61.
- Surface, L.E. et al. (2016) Cell Rep 14, 1142-55.
- Millar, C.B. et al. (2006) Genes Dev 20, 711-22.
- Ishibashi, T. et al. (2009) Biochemistry 48, 5007-17.
- Valdés-Mora, F. et al. (2012) Genome Res 22, 307-21.
- Sarcinella, E. et al. (2007) Mol Cell Biol 27, 6457-68.
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