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suggest that pH2AX alone or better in combination with MAP17 (show PDZK1IP1 Proteins) may become a novel and valuable prognostic biomarker for patients with laryngeal carcinoma treated with preservation approaches.
The findings demonstrate that RNF168 couples PALB2-dependent homologous recombination to H2A ubiquitylation to promote DNA repair and preserve genome integrity.
Data show that co-treated with vincristine and XL019, a inhibitor of JAK2 and P-glycoprotein (P-gp), up-regulated expression of p21 and phosphorylated H2A histone family, member X (pH2AX).
The bile acid receptor (show NR1H4 Proteins) TGR5 (show GPBAR1 Proteins), inducible nitric oxide synthase (iNOS (show NOS2 Proteins)) and gamma-histone family 2A variant (gamma-H2AX) are up-regulated.
Co-localization of gammaH2AX and 53BP1 (show TP53BP1 Proteins) indicates promotion of (in)effective nonhomologous end-joining repair mechanisms at sites of DSB. Moreover, gammaH2AX/53BP1 (show TP53BP1 Proteins) foci distribution presumably reveals a non-random spatial organization of the genome in MDS (show PAFAH1B1 Proteins) and AML (show RUNX1 Proteins).
Cyclin F (show CCNF Proteins)-mediated degradation of SLBP (show SLBP Proteins) limits H2A.X accumulation and apoptosis upon genotoxic stress in G2 cell cycle checkpoint.
study demonstrates that the individual and combined expression patterns of the DDR (show DDR1 Proteins) molecules PARP1 (show PARP1 Proteins), gammaH2AX, BRCA1, and BRCA2 (show BRCA2 Proteins) could be predictive of the prognosis of STS (show STS Proteins) patients and suggests that controlling the activity of these DDR (show DDR1 Proteins) molecules could be employed in new therapeutic stratagems for the treatment of STS (show STS Proteins)
Further analysis suggested that H2AX, a PARP-1 (show PARP1 Proteins) protein interaction partner, was coordinated with PARP-1 (show PARP1 Proteins) in hepatocellular carcinoma tumorigenesis. Overall, some new characteristics of PARP-1 (show PARP1 Proteins) expression were noted in the Zhuang population. PARP-1 (show PARP1 Proteins) is a novel promising diagnostic marker for hepatocellular carcinoma in the Southern Chinese Zhuang population
we found that gamma-H2AX foci at chromosome boundaries after carbon-ion irradiation contain DNA double strand breaks undergoing DNA-end resection, which promotes repair utilizing microhomology mediated end-joining during translocation.
this study demonstrates an early DDR (show DDR1 Proteins) defect of attenuated gammaH2AX signals in G0/G1 phase HGPS (show Zmpste24 Proteins) cells and provides a plausible connection between H3K9me3 loss and DDR (show DDR1 Proteins) deficiency.
Our data show that gammaH2AFX enrichment extends as far as 9-15 Mb of the annotated genomic sequence of the q-arms of the translocated chromosomal trivalents and that both gammaH2AFX and H3.3 levels are reduced over the X chromosome. Our data are also suggestive of an asymmetry in gammaH2AFX and H3.3 enrichment with a bias toward the non-translocated homolog.
Results suggest activation of H2AX via promoter demethylation in specific populations of basal mammary cells that is induced by a signal from neighboring luminal cells with hyper STAT5 (show STAT5A Proteins) activity.
A report on a role of H2AX in non-homologous end joining that repairs a site-specific chromosomal DNA double strand breaks
The SAGA deubiquitinase activity was required for optimal irradiation-induced gammaH2AX formation, and failure to remove H2BK120ub inhibits ATM (show ATM Proteins)- and DNAPK (show PRKDC Proteins)-induced gammaH2AX formation.
The authors observe that persistent accumulation of reactive oxygen species, due to a deficient JunD-/Nrf2-antioxidant response, reduces H2AX protein levels. This effect is mediated by an enhanced interaction of H2AX with the E3 ubiquitin ligase RNF168, which is associated with H2AX poly-ubiquitination and promotes its degradation by the proteasome.
TRAF6 (show TRAF6 Proteins) and H2AX overexpression and gammaH2AX-mediated HIF1alpha (show HIF1A Proteins) enrichment in the nucleus of cancer cells lead to overactivation of HIF1alpha (show HIF1A Proteins)-driven tumorigenesis, glycolysis and metastasis.
The findings highlight specific non-overlapping functions of PARP1 (show PARP1 Proteins) and PARP2 (show PARP2 Proteins) at H2AX-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 (show PARP1 Proteins) in nonhomologous end-joining-deficient cells.
Unlike directly induced DSBs, secondary DSBs were not efficiently repaired, although Rad51 (show RAD51 Proteins) and 53BP1 (show TP53BP1 Proteins) were recruited to these sites. H2AX was dramatically stabilized in response to DSBs directly caused by gamma-rays, enabling gammaH2AX foci formation and DSB repair, whereas H2AX was barely stabilized in response to secondary DSBs, in which gammaH2AX foci were small and DSBs were not efficiently repaired
this study shows that T cells and thyrocytes in a mouse model of thyrocyte hyperplasia has foci of phosphorylated histone protein H2A.X, indicative of cellular senescence
These findings suggest a dimerize-then-rearrange model for H2A-H2B dimers.
Findings reveal that XH2AX has a specific role in anterior neural formation of Xenopus, which is mediated through phosphorylation of XH2AX at Thr (show TRH Proteins)(16) by Chk1 (show CHEK1 Proteins).
H2Ax phosphorylated protein was detected in in parthenogenetically activated, in vitro fertilized and cloned bovine embryos.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a member of the histone H2A family, and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif.
, histone H2A.x
, histone 5 protein 2ax
, histone H2A type 1