Histone H2A.Z Antibody #2718
- WB
- IP
- IF
Supporting Data
| REACTIVITY | H M R Mk Z |
| SENSITIVITY | Endogenous |
| MW (kDa) | 14 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
- Z-Zebrafish
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:200 - 1:800 |
Storage
Protocol
Specificity / Sensitivity
Histone H2A.Z Antibody detects endogenous levels of histone H2A.Z protein. The antibody does not cross-react with other histone proteins, including histone H2A.
Species Reactivity:
Human, Mouse, Rat, Monkey, Zebrafish
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Chicken, Xenopus, Bovine
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human histone H2A.Z. Antibodies are purified by protein A and peptide affinity chromatography.
Background
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).
- 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.
Limited Uses
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