Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
Co-localization of gammaH2AX and 53BP1 (show TP53BP1 ELISA Kits) indicates promotion of (in)effective nonhomologous end-joining repair mechanisms at sites of DSB. Moreover, gammaH2AX/53BP1 (show TP53BP1 ELISA Kits) foci distribution presumably reveals a non-random spatial organization of the genome in MDS (show PAFAH1B1 ELISA Kits) and AML (show RUNX1 ELISA Kits).
Cyclin F (show CCNF ELISA Kits)-mediated degradation of SLBP (show SLBP ELISA Kits) 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 ELISA Kits) molecules PARP1 (show PARP1 ELISA Kits), gammaH2AX, BRCA1, and BRCA2 (show BRCA2 ELISA Kits) could be predictive of the prognosis of STS (show STS ELISA Kits) patients and suggests that controlling the activity of these DDR (show DDR1 ELISA Kits) molecules could be employed in new therapeutic stratagems for the treatment of STS (show STS ELISA Kits)
Further analysis suggested that H2AX, a PARP-1 (show PARP1 ELISA Kits) protein interaction partner, was coordinated with PARP-1 (show PARP1 ELISA Kits) in hepatocellular carcinoma tumorigenesis. Overall, some new characteristics of PARP-1 (show PARP1 ELISA Kits) expression were noted in the Zhuang population. PARP-1 (show PARP1 ELISA Kits) 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 ELISA Kits) defect of attenuated gammaH2AX signals in G0/G1 phase HGPS (show Zmpste24 ELISA Kits) cells and provides a plausible connection between H3K9me3 loss and DDR (show DDR1 ELISA Kits) deficiency.
Data indicate an important role for histone H2A.X (H2AX) Tyr39 phosphorylation in gamma-H2A.X formation and cancer progression.
we suggest that the XAB2 (show XAB2 ELISA Kits) complex mediates DNA damage response events important for the end resection step of homologous recombination , and speculate that its adjacent-localization relative to double-strand break marked by gH2AX is important for this function
the epithelial-mesenchymal transition-related transcription factor Twist1 (show TWIST1 ELISA Kits) cooperates with Slug (show SNAI2 ELISA Kits) to regulate EMT (show ITK ELISA Kits) upon H2A.X Loss.
Upon DNA damage, an increase in the levels of chromatin bound motor protein nuclear myosin 1 (NM1 (show MYO1C ELISA Kits)) ensues, which appears to be functionally linked to Upsilon-H2AX signaling.
The SAGA deubiquitinase activity was required for optimal irradiation-induced gammaH2AX formation, and failure to remove H2BK120ub inhibits ATM (show ATM ELISA Kits)- and DNAPK (show PRKDC ELISA Kits)-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 ELISA Kits) and H2AX overexpression and gammaH2AX-mediated HIF1alpha (show HIF1A ELISA Kits) enrichment in the nucleus of cancer cells lead to overactivation of HIF1alpha (show HIF1A ELISA Kits)-driven tumorigenesis, glycolysis and metastasis.
The findings highlight specific non-overlapping functions of PARP1 (show PARP1 ELISA Kits) and PARP2 (show PARP2 ELISA Kits) at H2AX-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 (show PARP1 ELISA Kits) in nonhomologous end-joining-deficient cells.
Unlike directly induced DSBs, secondary DSBs were not efficiently repaired, although Rad51 (show RAD51 ELISA Kits) and 53BP1 (show TP53BP1 ELISA Kits) 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
The role of H2AX phosphorylation and H3K56 acetylation on normal stem cell response to radiation
H2AX knockout mice showed cell-autonomous anaemia and erythroid dysplasia, mimicking dyserythropoiesis in MDS (show MECOM ELISA Kits).
These data suggest a role for FoxO3a in the maintenance of genome integrity in response to DNA damage that is mediated by H2AX via yet unknown mechanisms.
overexpression of TIPRL promotes phosphorylation of H2AX, and increases gamma-H2AX positive foci in response to DNA damage, whereas knockdown of TIPRL inhibits gamma-H2AX phosphorylation
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 ELISA Kits)(16) by Chk1 (show CHEK1 ELISA Kits).
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