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anti-Human H2AFZ Antikörper:
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Human Polyclonal H2AFZ Primary Antibody für ChIPSeq, ChIP - ABIN4889649
El Gazzar, Liu, Yoza, McCall: Dynamic and selective nucleosome repositioning during endotoxin tolerance. in The Journal of biological chemistry 2010
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Human Polyclonal H2AFZ Primary Antibody für ChIPSeq, ChIP - ABIN2668307
Lodhi, Kossenkov, Tulin: Bookmarking promoters in mitotic chromatin: poly(ADP-ribose)polymerase-1 as an epigenetic mark. in Nucleic acids research 2014
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Mammalian Monoclonal H2AFZ Primary Antibody für - ABIN1304703
Satterlee, Beckel-Mitchener, McAllister, Procaccini, Rutter, Tyson, Chadwick: Community resources and technologies developed through the NIH Roadmap Epigenomics Program. in Methods in molecular biology (Clifton, N.J.) 2014
H2A.Z associates with epigenetic gene activation in prostate cancer.Acetylated H2A.Z role in activation of newly formed enhancers in prostate cancer.
The present study demonstrated that H2A.Z is overexpressed in ICC and expression of H2A.Z correlated with poor prognosis in patients with ICC. H2A.Z regulated cell proliferation in vitro and in vivo via H2A.Z/S-phase kinase-associated protein 2/p27 (zeige PAK2 Antikörper)/p21 (zeige CDKN1A Antikörper) signaling.
study identifies GAS41 as a histone acetylation reader that promotes histone H2A.Z deposition in non-small cell lung cancer.
Two possible modes of pioneering associated with combinations of H2A.Z and p300/CBP (zeige CREBBP Antikörper) at nucleosome-occupied enhancers.
Results indicate that accumulation of H2A.Z within repressed genes can also be a consequence of the repression of gene transcription rather than an active mechanism required to establish the repression.
Findings suggest the oncogenic potential of H2A.Z.1 in liver tumorigenesis and that it plays established role in accelerating cell cycle transition and EMT (zeige ITK Antikörper) during hepatocarcinogenesis.
Crystal structure results show that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.
Monoubiquitination of histone H2B blocks eviction of histone variant H2A.Z from inducible enhancers.
Thus, PWWP2A is a novel H2A.Z-specific multivalent chromatin binder providing a surprising link between H2A.Z, chromosome segregation, and organ development.
SMYD3 (zeige SMYD3 Antikörper)-mediated H2A.Z.1K101 dimethylation activates cyclin A1 (zeige CCNA1 Antikörper) expression and contributes to driving the proliferation of breast cancer cells.
The data also suggest that H2A.Z restricts transcription, which is moderated by ANP32e (zeige ANP32E Antikörper) at the promoter and gene bodies of expressed genes. Thus, ANP32e (zeige ANP32E Antikörper), through inhibition of PP2A (zeige PPP2R2B Antikörper), is required for nucleosomal inclusion of H2A.Z and the regulation of gene expression
In contrast to H2A-interacting proteins, the H2A.Z-interacting proteins are involved in transcriptional regulation. We found that the transcription factor Osr1 (zeige OSR1 Antikörper) interacts with H2A.Z both in vitro and in vivo. It also mediates H2A.Z incorporation to a large number of target sites and regulates gene expression
This study reveals an antagonistic relationship between H2A.Z.1ub and BRD2 (zeige BRD2 Antikörper) to regulate the transcriptional balance at bivalent genes to enable proper execution of developmental programs.
Embryonic stem cell BAF (zeige BANF1 Antikörper) is required for normal H2A.Z localization in these cells, suggesting BAF (zeige BANF1 Antikörper) either stabilizes H2A.Z containing nucleosomes or promotes subnucleosome to nucleosome conversion by facilitating H2A.Z deposition.
Study mapped H2A.Z genome-wide in embryonic stem cells and neural progenitors; H2A.Z is deposited at promoters and enhancers, and correlates strongly with H3K4 methylation. H2A.Z is present at poised promoters with bivalent chromatin and at active promoters with H3K4 methylation, but is absent from stably repressed promoters that are enriched for H3K27 trimethylation.
our work suggests that the divergent residues in the H2A.Z acidic patch comprise a unique domain that couples control of chromatin dynamics to the regulation of developmental gene expression patterns during lineage commitment.
Data propose that H2A.Z mediates such contrasting activities by acting as a general facilitator that generates access for a variety of complexes, both activating and repressive.
The variant histone H2A.Z and the winged helix transcription factor (zeige FOXC1 Antikörper) Foxa2 (zeige FOXA2 Antikörper) both act to regulate nucleosome depletion and gene activation, thus promoting embryonic stem cell differentiation, whereas DNA methylation (zeige HELLS Antikörper) promotes nucleosome occupation and suppresses gene expression.
incorporation of the histone variant H2A.Z at the promoter regions of PPARgamma (zeige PPARG Antikörper) target genes by p400 (zeige ITPR1 Antikörper)/Brd8 (zeige BRD8 Antikörper) is essential to allow fat cell differentiation
In mouse trophoblast stem cells, the amount of histone H2A.Z at promoters decreased during S phase, coinciding with homotypic (H2A.Z-H2A.Z) nucleosomes flanking the TSS (zeige RPL38 Antikörper) becoming heterotypic (H2A.Z-H2A).
Depletion of H2A.Z by RNA interference perturbs Xenopus laevis development at gastrulation leading to embryos with malformed, shortened trunks.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene encodes a replication-independent member of the histone H2A family that is distinct from other members of the family. Studies in mice have shown that this particular histone is required for embryonic development and indicate that lack of functional histone H2A leads to embryonic lethality.
, histone H2A.Z
, H2A histone family, member Z
, H2A histone family, member V
, histone H2A.Z-like
, histone H2A.Zl2
, histone H2AF