Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|Ch, H, Zebrafish, Rb, R, Xn, M||WB||Sh||Affinity Purified||Polyclonal Antibody|
|Presentation||Purified sheep polyclonal IgG in PBS, pH 7.4 containing with 1% BSA with 0.02% sodium azide.|
|Application||Use Anti-Histone H2A.Z Antibody (Sheep Polyclonal Antibody) validated in WB to detect Histone H2A.Z also known as H2A histone family member Z, H2AZ histone.|
|Safety Information according to GHS|
|Material Size||100 µg|
|Anti-Histone H2A.Z - 2459505||2459505|
|Anti-Histone H2A.Z - 2326439||2326439|
|Anti-Histone H2A.Z - NG1590601||NG1590601|
|Anti-Histone H2A.Z - NG1940773||NG1940773|
|Anti-Histone H2A.Z -2726198||2726198|
|Anti-Histone H2A.Z -2746235||2746235|
|Anti-Histone H2A.Z Polyclonal Antibody||2887687|
|Anti-Histone H2A.Z Polyclonal Antibody||2949950|
|Reference overview||Pub Med ID|
|The histone variant composition of centromeres is controlled by the pericentric heterochromatin state during the cell cycle.|
Boyarchuk, E; Filipescu, D; Vassias, I; Cantaloube, S; Almouzni, G
Journal of cell science 127 3347-59 2014
Correct chromosome segregation requires a unique chromatin environment at centromeres and in their vicinity. Here, we address how the deposition of canonical H2A and H2A.Z histone variants is controlled at pericentric heterochromatin (PHC). Whereas in euchromatin newly synthesized H2A and H2A.Z are deposited throughout the cell cycle, we reveal two discrete waves of deposition at PHC - during mid to late S phase in a replication-dependent manner for H2A and during G1 phase for H2A.Z. This G1 cell cycle restriction is lost when heterochromatin features are altered, leading to the accumulation of H2A.Z at the domain. Interestingly, compromising PHC integrity also impacts upon neighboring centric chromatin, increasing the amount of centromeric CENP-A without changing the timing of its deposition. We conclude that the higher-order chromatin structure at the pericentric domain influences dynamics at the nucleosomal level within centromeric chromatin. The two different modes of rearrangement of the PHC during the cell cycle provide distinct opportunities to replenish one or the other H2A variant, highlighting PHC integrity as a potential signal to regulate the deposition timing and stoichiometry of histone variants at the centromere.
|Pancreatic islet enhancer clusters enriched in type 2 diabetes risk-associated variants.|
Pasquali, L; Gaulton, KJ; Rodríguez-Seguí, SA; Mularoni, L; Miguel-Escalada, I; Akerman, I; Tena, JJ; Morán, I; Gómez-Marín, C; van de Bunt, M; Ponsa-Cobas, J; Castro, N; Nammo, T; Cebola, I; García-Hurtado, J; Maestro, MA; Pattou, F; Piemonti, L; Berney, T; Gloyn, AL; Ravassard, P; Gómez-Skarmeta, JL; Müller, F; McCarthy, MI; Ferrer, J
Nature genetics 46 136-43 2014
Type 2 diabetes affects over 300 million people, causing severe complications and premature death, yet the underlying molecular mechanisms are largely unknown. Pancreatic islet dysfunction is central in type 2 diabetes pathogenesis, and understanding islet genome regulation could therefore provide valuable mechanistic insights. We have now mapped and examined the function of human islet cis-regulatory networks. We identify genomic sequences that are targeted by islet transcription factors to drive islet-specific gene activity and show that most such sequences reside in clusters of enhancers that form physical three-dimensional chromatin domains. We find that sequence variants associated with type 2 diabetes and fasting glycemia are enriched in these clustered islet enhancers and identify trait-associated variants that disrupt DNA binding and islet enhancer activity. Our studies illustrate how islet transcription factors interact functionally with the epigenome and provide systematic evidence that the dysregulation of islet enhancers is relevant to the mechanisms underlying type 2 diabetes.
|Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks.|
Zilberman, Daniel, et al.
Nature, 456: 125-9 (2008) 2008
Eukaryotic chromatin is separated into functional domains differentiated by post-translational histone modifications, histone variants and DNA methylation. Methylation is associated with repression of transcriptional initiation in plants and animals, and is frequently found in transposable elements. Proper methylation patterns are crucial for eukaryotic development, and aberrant methylation-induced silencing of tumour suppressor genes is a common feature of human cancer. In contrast to methylation, the histone variant H2A.Z is preferentially deposited by the Swr1 ATPase complex near 5' ends of genes where it promotes transcriptional competence. How DNA methylation and H2A.Z influence transcription remains largely unknown. Here we show that in the plant Arabidopsis thaliana regions of DNA methylation are quantitatively deficient in H2A.Z. Exclusion of H2A.Z is seen at sites of DNA methylation in the bodies of actively transcribed genes and in methylated transposons. Mutation of the MET1 DNA methyltransferase, which causes both losses and gains of DNA methylation, engenders opposite changes (gains and losses) in H2A.Z deposition, whereas mutation of the PIE1 subunit of the Swr1 complex that deposits H2A.Z leads to genome-wide hypermethylation. Our findings indicate that DNA methylation can influence chromatin structure and effect gene silencing by excluding H2A.Z, and that H2A.Z protects genes from DNA methylation.
|A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome.|
Park, Young-Jun, et al.
J. Biol. Chem., 279: 24274-82 (2004) 2004
Nucleosomes are highly dynamic macromolecular complexes that are assembled and disassembled in a modular fashion. One important way in which this dynamic process can be modulated is by the replacement of major histones with their variants, thereby affecting nucleosome structure and function. Here we use fluorescence resonance energy transfer between fluorophores attached to various defined locations within the nucleosome to dissect and compare the structural transitions of a H2A.Z containing and a canonical nucleosome in response to increasing ionic strength. We show that the peripheral regions of the DNA dissociate from the surface of the histone octamer at relatively low ionic strength, under conditions where the dimer-tetramer interaction remains unaffected. At around 550 mm NaCl, the (H2A-H2B) dimer dissociates from the (H3-H4)(2) tetramer-DNA complex. Significantly, this latter transition is stabilized in nucleosomes that have been reconstituted with the essential histone variant H2A.Z. Our studies firmly establish fluorescence resonance energy transfer as a valid method to study nucleosome stability, and shed new light on the biological function of H2A.Z.
|Histone H2A variants H2AX and H2AZ.|
Redon, Christophe, et al.
Curr. Opin. Genet. Dev., 12: 162-9 (2002) 2002
Two of the nucleosomal histone families, H3 and H2A, have highly conserved variants with specialized functions. Recent studies have begun to elucidate the roles of two of the H2A variants, H2AX and H2AZ. H2AX is phosphorylated on a serine four residues from the carboxyl terminus in response to the introduction of DNA double-strand breaks, whether these breaks are a result of environmental insult, metabolic mistake, or programmed process. H2AZ appears to alter nucleosome stability, is partially redundant with nucleosome remodeling complexes, and is involved in transcriptional control.