Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human H2AFZ Antikörper:
anti-Mouse (Murine) H2AFZ Antikörper:
anti-Rat (Rattus) H2AFZ Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
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
Show all 9 Pubmed References
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
Show all 2 Pubmed References
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
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.
Results suggest that the N-terminal tail of H2A.Z makes distinctively different contributions to epigenetic events.
the H2AFZ gene may confer a risk for schizophrenia and contribute to the impairment of executive function in Han Chinese patients with schizophrenia.
The 2.7-A-resolution crystal structure of the human YL1 (zeige VPS72 Antikörper)-H2A.Z-H2B complex shows that YL1 (zeige VPS72 Antikörper) binding, similarly to ANP32E (zeige ANP32E Antikörper) binding, triggers an extension of the H2A.Z alphaC helix.
H2A.Z removal from chromatin is the primary function of INO80 (zeige INO80 Antikörper) and ANP32E (zeige ANP32E Antikörper) in promoting homologous recombination.
Results demonstrated male-selective association of the H2AFZ gene with schizophrenia, and that modification of the H2AFZ signaling pathway warrants further study in terms of the pathophysiology of schizophrenia
Dynamic modulation of H2A.Z exchange and removal by Anp32e (zeige ANP32E Antikörper) reveals the importance of the nucleosome surface and nucleosome dynamics in processing the damaged chromatin template during DSB repair.
The findings implicate H2A.Z.2 as a mediator of cell proliferation and drug sensitivity in malignant melanoma.
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).
It was shown that Ring1B (zeige RNF2 Antikörper) interacted with multiple complexes in embryonic stem cells. Although H2A.Z co-localized with Eed (zeige EED Antikörper), Ring1B (zeige RNF2 Antikörper) and CpG islands in chromatin, H2A.Z still blanketed polycomb (zeige CBX2 Antikörper) target loci in the absence of Suz12 (zeige SUZ12 Antikörper), Eed (zeige EED Antikörper), or Ring1B (zeige RNF2 Antikörper).
Studies indicate that the unique chromatin landscape also includes a second histone variant, H2A.Z.
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.
H2A histone family, member Z
, H2A histone family, member V
, H2A histone family member V
, histone H2A.Z
, H2AZ histone
, histone H2AF
, histone H2A.Z-like
, histone H2A.Zl2