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Validated All-in-One™ qPCR Primer for H2AX(NM_002105.2) Search again
Product ID:
HQP008703
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
H2A.X, H2A/X, H2AFX
Gene Description:
H2A.X variant histone
Target Gene Accession:
NM_002105.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- The site of very early phosphorylation of H2A.X (obtained from human skin fibroblast cells)in response to low-dose radiation was identified by mass spectrometry.
- During the end-joining reaction H2AX is phosphorylated at Ser-139 as detected by immunoblot with specific antibodies and phosphorylation is inhibited by wortmannin, in vitro the DNA end-joining reaction appears to be independent of H2AX phosphorylation.
- H2AX has low diffusional mobility in the nucleus
- H2AX is involved in a pathway with NFBD1, 53BP1, and Chk2 in recruitment of repair and signaling proteins to sites of DNA damage
- phosphorylation of and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes
- Sex chromosomes of histone H2AX-deficient spermatocytes don't form a sex body or initiate MSCI, and show defects in meiotic pairing. H2AX is required for the chromatin remodeling and associated silencing in male meiosis.
- Migration of repair and signalling proteins to double-stranded breaks is not abrogated in H2AX(-/-) cells, or in those that have been reconstituted with H2AX mutants that eliminate phosphorylation.
- Fibroblasts from patients with Huntington disease and spinocerebellar ataxia-2 showed significant phosphorylation.
- a role in repairing DNA double-stranded breaks in human cells
- DNA-PK can be activated by nucleosomes through the ability of Ku to bind to the ends of nucleosomal DNA, and that the activated DNA-PK is capable of phosphorylating H2AX within the nucleosomes
- MDC1 couples DNA ds-break recognition by NBS1 with its H2AFX-dependent chromatin retention.
- chromatin restructuring mediated by H2AX phosphorylation concentrates DNA repair/signaling factors and tethers DNA ends together [review]
- DNA-PK, ATM and possibly other kinases implicated in H2AX phosphorylation.
- we show a requirement for Rad17 and Hus1 to induce G(2) arrest as well as Vpr-induced phosphorylation of histone 2A variant X (H2AX) and formation of nuclear foci containing H2AX and breast cancer susceptibility protein 1
- ATM, Artemis, and proteins locating to gamma-H2AX foci have roles in double-strand break rejoining
- Histone gamma-H2AX promotes binding of nuclear DNA helicase II to transcriptionally stalled sites on chromosomal DNA.
- data are consistent with the notion that H2AX phosphorylation observed throughout S phase reflects formation of double-strand breaks due to the collision of replication forks with the UV-induced primary DNA lesions
- In this communication, we present the first evidence that heat shock induces the phosphorylated form of histone H2AX, which is thought to be generated at the chromatin proximal to DSB sites
- Werner syndrome protein co-localizes and associates with gamma H2AX
- untreated melanoma cells express significantly greater numbers of gammaH2AX foci than do untreated melanocytes
- Phosphorylated H2AX is a sensitive assay for the presence of double strand breaks.
- DNA-PK activity is required for the increased expression of H2AX in iradiated cells under hypertonic conditions.
- Even in the absence of DNA damage, phosphorylation of H2AX in normal cell cycle progression may contribute to maintenance of genomic integrity.
- these data implicate BRCA1 and the H2AX kinase in replication of facultative heterochromatin on the inactive X chromosome
- H2AX is not a target gene for 11q23 deletions in MCL
- Frequency of activated ATM and phosphorylated H2AX molecules, per apoptotic cell, is comparable.
- phosphorylated histone H2AX foci persist if DNA breaks are rejoined
- increased histone H2AX phosphorylation also occurred outside of double-strand break sites after exposure to ionizing radiation
- 2-deoxy-D-glucose reduces the level of constitutive activation of ATM and phosphorylation of histone H2AX
- XPF is required to form gamma-H2AX and likely double strand breaks in response to interstrand crosslinks in human cells
- H2AX phosphorylation in G(1) cells depends on nucleotide excision repair factors that may expose the S-139 site to kinase activity, is not due to DNA double-strand breaks, and plays a larger role in UV-induced signal transduction than previously realized
- H2AX phosphorylation on Ser-139 in cells untreated by genotoxic agents is cell-cycle phase specific and attenuated by scavenging reactive oxygen species
- The higher level of constitutive H2AX phosphorylation in cells harbouring wt tumour protein p53 may thus indicate that tumour protein p53 plays a role in facilitating histone H2AX phosphorylation.
- A model is proposed for non-targeted (bystander) signaling leading to gamma H2AX foci induction in irradiated primary astrocytes and glioma cells.
- These results demonstrate that neither RPA hyper-phosphorylation nor H2AX are required for the formation in RPA intra-nuclear foci in response to DNA damage/replicational stress.
- We determined independently that those siblings with mean numbers of foci per cell in the range of ATM heterozygotes carried the mutant allele, while both siblings with a normal number of foci per cell after irradiation had normal alleles.
- H2AX phosphorylation and two other collaborating proteins, Rad50 and 53BP1, were generated in spermatozoa after H(2)O(2) exposure; oxidative stress can induce H2AX phosphorylation in human spermatozoa through double strand break induction
- induction of oxidative stress in human peripheral blood leukocytes by phorbol myristate acetate (PMA) was associated with intense phosphorylation of histone H2AX
- data support a model in which the size and distribution of H2AX clusters define the boundaries of gamma-H2AX spreading and also may provide a platform for the immediate and robust response observed after DNA damage
- Genotoxic responses to ultraviolet radiation, like increase in the phosphorylation of histone H2AX, induction of p53 protein and binding of this protein to its DNA consensus sequence, were all decreased on the restrictive substrate.
- The levels of CAA and CHP in lymphocytes were increased many-fold during their stimulation. This increase was paralleled by the rise in extent of endogenously generated ROS.
- Heat shock does not induce gammaH2AFX foci formation but protects cells from methylnitrososguanidine.
- We propose a model that perturbed gap-filling synthesis following dual incision in NER generates single-strand DNA gaps and hence initiates H2AX phosphorylation.
- These findings demonstrate that exposure of crude oil to sunlight makes the water soluble fraction phototoxic, generating DNA double strand breaks accompanying the appearance of gamma-H2AX in human skin cells.
- data support the hypothesis that genetic variation in the H2AFX gene influences genetic susceptibility or resistance to some subtypes of non-Hodgkin lymphoma by contributing to the maintenance of genome stability.
- implicate ataxia telangiectasia mutated as the phosphoinositide 3-kinase related protein kinases that phosphorylates H2AX in response to DNA damage caused by cigarette smoke
- This is the first report of high ATM-Chk2 kinase activation and its linkage to replication defects in a Bloom syndrome model.
- phosphorylated histone H2AX in differentiated somatic cells differed from the cells
- Data suggest that the sequential acetylation and ubiquitination of H2AX by TIP60-UBC13 promote enhanced histone dynamics, which in turn stimulate a DNA damage response.
- histone H2AX inhibits transcription through phosphorylation and can decrease chromatin movement at DSBs and frequency of misjoining of DNA ends
- We conclude that the method of detection of residual gammaH2AX after in vitro irradiation of lymphocytes and monocytes was simple, reproducible, and sensitive.
- MCPH1 functions in an H2AX-dependent but MDC1-independent pathway in response to DNA damage
- gammaH2AX is regarded as forming a platform for the recruitment or retention of other DNA repair and signaling molecules
- RNF8 is required for H2AX ubiquitylation after DNA damage.
- Copy number alterations of the H2AFX gene in sporadic breast cancer patients.
- Rvb1 is critical for the dephosphorylation of phospho-H2AX due to the role of Rvb1 in maintaining the histone acetyltransferase activity of Tip60/NuA4
- Present data represent the first evidence for the role of NBS1 tandem BRCT domains in gamma-H2AX recognition, and could explain the severe phenotype observed in 657del5/R215W NBS patients.
- Data establish FACT as the major regulator involved in H2AX exchange process that is modulated by H2AX phosphorylation and Spt16 ADP-ribosylation.
- X-ray-induced gamma-H2AX foci in G0 lymphocyte nuclei contain more than one DSB and that the increasing number of DSBs per gamma-H2AX repair factory lead to an increased rate of misrepair.
- Unlikely that the H2AX mutations are a common genetic cause of spermatogenic impairment in idiopathic infertile men.
- A three-protein PP4 phosphatase complex in mammalian cells, containing PP4C, PP4R2, and PP4R3beta, that specifically dephosphorylates ATR-mediated gamma-H2AX generated during DNA replication, is described.[
- results show that DNA replication stress rapidly leads to increased soluble H2AX and that non-chromatin-associated H2AX can sensitize cells to undergo apoptosis
- Studies summarize mechanisms by which H2AX functions during V(D)J recombination to coordinate DSB repair with cellular proliferation and survival to prevent translocations and suppress lymphomagenesis.
- ATM, Mre11, and Rad50 are required for survival after replication fork stalling, whereas Nbs1 and H2AX are inconsequential.
- These findings suggest that nuclear activation of Chk2 by TRAIL acts as a positive feedback loop involving the mitochondrion-dependent activation of caspases, independently of p53.
- Histone H2AX phosphorylation on a serine four residues from the carboxyl terminus is a sensitive marker for DNA double-strand breaks, which may lead to cancer [REVIEW]
- WSTF phosphorylates Tyr 142 of H2A.X, and WSTF activity has an important role in regulating several events that are critical for the DNA damage response
- ABCG2 protects ES cells from PPIX accumulation during colony expansion, and that p53 and gammaH2AX acts as a downstream checkpoint of ABCG2-dependent defense machinery in order to maintain the self-renewal of ES cells.
- BRCA1, ATR and gammaH2AX in the human may be part of a system which signals unsynapsed chromosomes at pachytene and may lead to their silencing.