Product Pathways - Chromatin Regulation / Epigenetics
Histone H2A.Z Antibody #2718
|W IP IF-IC||H M R Mk Z (C) (X) (B)||Endogenous||14||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey C=Chicken X=Xenopus Z=Zebrafish B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
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.
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.
Western blot analysis of HeLa, NIH/3T3, H-4-II-E and COS cell lysates, in addition to 10 ng of recombinant H2A (rH2A) and H2A.Z (rH2A.Z) protein, using Histone H2A.Z Antibody #2718 (upper) and Histone H2A Antibody II #2578 (lower).
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. cerivisiae), 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, 680-687.
- Raisner, R.M. and Madhani, H.D. (2006) Curr. Opin. Genet. Dev. 16, 119-124.
- Mizuguchi, G. et al. (2004) Science 303, 343-348.
- Kusch, T. et al. (2004) Science 306, 2084-2087.
- Ruhl, D.D. et al. (2006) Biochemistry 45, 5671-5677.
- Suto, R.K. et al. (2000) Nat. Struct. Bio.l 7, 1121-1124.
- Fan, J.Y. et al. (2004) Mol. Cell 16, 655-661.
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For Research Use Only. Not For Use In Diagnostic Procedures.