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Human Monoclonal APEX1 Primary Antibody for ChIP, GS - ABIN4889971
Fishel, Seo, Smith, Kelley: Imbalancing the DNA base excision repair pathway in the mitochondria; targeting and overexpressing N-methylpurine DNA glycosylase in mitochondria leads to enhanced cell killing. in Cancer research 2003
Show all 88 Pubmed References
Human Polyclonal APEX1 Primary Antibody for BP, ChIP - ABIN151028
Briegert, Kaina: Human monocytes, but not dendritic cells derived from them, are defective in base excision repair and hypersensitive to methylating agents. in Cancer research 2007
Show all 63 Pubmed References
Polyclonal APEX1 Primary Antibody for IHC (fro), IHC (p) - ABIN540784
Yang, Chen, Zhang, Huang, Zhang: Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA. in The Journal of biological chemistry 2007
Show all 5 Pubmed References
Human Polyclonal APEX1 Primary Antibody for IHC (p), IHC - ABIN257862
Demple, Herman, Chen: Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. in Proceedings of the National Academy of Sciences of the United States of America 1992
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Arabidopsis thaliana Polyclonal APEX1 Primary Antibody for WB - ABIN6254847
Kangasjaervi, Lepistoe, Haennikaeinen, Piippo, Luomala, Aro, Rintamaeki: Diverse roles for chloroplast stromal and thylakoid-bound ascorbate peroxidases in plant stress responses. in The Biochemical journal 2008
Show all 7 Pubmed References
Human Polyclonal APEX1 Primary Antibody for IHC, WB - ABIN3015421
Xu, Zhang, Zhang, Meng, Zhang, Jiang, Xu, Van Meter, Seluanov, Gorbunova, Mao: SIRT6 rescues the age related decline in base excision repair in a PARP1-dependent manner. in Cell cycle (Georgetown, Tex.) 2015
Establishing Ref-1 inhibition as a promising therapeutic approach for ocular neovascularization.
hyperacetylation in xenografts caused secretion of Ac-APE1/Ref-1 into the blood, where the factor bound directly to RAGE in hyperacetylated tumor tissues. Hyperacetylation in the Triple-negative breast cancer xenografts induced strong inhibition of tumor growth and development, leading to apoptotic cell death
he lyase activity of hNTHL1, and the 3' diesterase activity of APE1, which had been seen as relatively dispensable, may have been preserved during evolution to enhance base excision repair (BER) in chromatin
For seven APE1 variants (R221C, N222H, R237A, G241R, M270T, R274Q, and P311S), conformational dynamics and catalytic activities were examined. The results made it possible to determine the kinetic mechanism underlying the interactions of the APE1 variants with DNA substrates, to calculate the rate constants of the elementary stages, and to identify the stages of the process affected by mutation.
APE1 expression is inversely correlated with cellular senescence in primary human fibroblasts. Low APE1 expression in patient cancer tissue also correlated with increased senescence.
the Ape1 N-terminal sequence is an important relay site for regulating the enzyme's activity on G4-telomeric sequences, and specific acetylatable lysine residues constitute key regulatory sites of Ape1 enzymatic activity dynamics at telomeres
Substrate specificity of human apurinic/apyrimidinic endonuclease APE1 in the nucleotide incision repair pathway has been reported.
expression of APE1 in hepatocellular carcinoma tissues and cells was significantly up-regulated, and its expression was significantly different from TNM staging and histopathological grading
Here the authors present evidence that Ape1 facilitates BRCA1-mediated homologous recombination repair (HR), while counteracting error-prone non-homologous end joining of DNA double-strand breaks.
Genetic and biochemical characterization of human AP endonuclease 1 mutants deficient in nucleotide incision repair activity.
carrying the allele T of XRCC1 rs1799782 polymorphism and the allele G of APEX rs1130409 polymorphism increased the risk of developing Paget's disease of bone.
This study suggested that APE1 rs1760944 polymorphism is associated with decreased risk of developing osteosarcoma and better survival of osteosarcoma patients.
It is reviewed what is known about the numerous APE1 cleavage reactions as well as the mechanistic features and activities that remain enigmatic with this essential multifaceted enzyme.
Data provide clear evidence that the rs3136817 polymorphism in APEX1 and a corresponding haplotype may be involved in breast cancer risk in the Han women of Northwest China.
A critical role for APE1 induction in activating the EGFR-STAT3 signaling axis.
Increased lung cancer risk was revealed in workers-carriers of homozygous minor genotype of genes OGG1] Ser326Cys (OR - 4.67, p = 0.007), APE1 Asp148Glu (OR = 1.82, p = 0.063) and XRCC1 Gln399Arg (OR = 2.86, p = 0.026).
Active-site residue His309 is found to be protonated based on pKa calculations and the higher conformational stability of the Ape1-DNA substrate complex compared to scenarios with neutral His309.
High APE1 expression is associated with resistance of glioblastoma cells to temozolomide.
Data confirm that C1D is not directly involved in repair of UV-damaged DNA; C1D appears to protects cells from oxidative stress (induced by UV irradiation or hydrogen peroxide oxidation) by regulating expression of DNA repair/transcription enzymes such as APEX1 or DDIT3. (C1D = nuclear receptor corepressor C1D; APEX1 = apurinic/apyrimidinic endodeoxyribonuclease-1; DDIT3 = DNA damage inducible transcript-3)
X-ray crystallographic structures of the human nuclease apurinic/apyrimidinic (AP) endonuclease 1 (APE1) in complex with its substrate target flanked by a 5' mismatch reveal how APE1 influences the conformations of a variety of different mismatched base pairs.
Study shows the methylation of the APE1 promoter and its role in mediating the functional effects of redox reactions induced by oxidative stress.
Meiosis progression and female age affect expression profile of DNA repair APEX1 gene in bovine oocytes.
prediction of the 3D structure of bovine AP lyase (BAP1); models of mutants showed substitution of Arg176-->Ala leads to the loss of DNA binding whereas mutation of Asp282-->Ala and His308-->Asn leads to a decrease in the enzymatic activity.
Ape1 knockout mice appeared hypothermic with persistent shivering associated with the loss of thermoregulatory serotonergic neurons.
We suggest that serum APE1/Ref-1 can be used to assess for myocardial injury in viral myocarditis without endomyocardial biopsy
AOM, a colorectal cancer carcinogen, generates damage to the mitochondrial genome, and the BER enzyme APE1 is required to maintain its integrity.
findings provide evidence that endogenous APE1 protects against ischemic infarction in both gray and white matter and facilitates the functional recovery of the central nervous system after mild stroke injury
Suppression of Ape1/Ref-1 redox function leads to an increased cell surface retention of IL-12 and enhances Th1 responses.
Is closely associated with upregulation of the Ref1/Nrf2 signalling pathway.
Results show the stimulatory effect of PARP-1 on APE1-dependent base excision repair (BER). PARP-1 and APE1 appear to have a functional interaction in BER since PARP-1 can stimulate the strand incision activity of APE1.
increases in APEX1 level confer protection against the murine paternal age effect, thus highlighting the role of APEX1 in preserving reproductive health with increasing age and in protection against genotoxin-induced mutagenesis in somatic cells
Endothelial cell tumor proliferation was found to be dependent on Apex-1 expression.
Expression of OGG1 and APEX1 was decreased at 3h after last exposure to Aroclor 1254 and only the expression level of APEX1 was recovered at 24-h after, so inhibition of DNA repair can be a potential mode of action of Aroclor 1254 gonadal toxicity.
Data indicate that the endonuclease activity of APE1 is required for class switch recombination (CSR).
These results suggest that mitochondrial APE1/Ref-1 is contributed to the protective role to protein kinase C-induced mitochondrial dysfunction in endothelial cells.
Spinal motor neurones down-regulate APE1 upon oxidative stress. This property renders motor neurones susceptible to continuous challenge of oxidative stress in pathological conditions.
The reductive activation of endothelial SIRT1 by APE1/Ref-1 mediates the effect of APE1/Ref-1 on eNOS acetylation, promoting endothelium-derived NO and endothelium-dependent vasorelaxation.
Together, these data show that the expression of APE1 is crucial for efficient transcription of ribosomal genes.
Ape1, an enzyme required for processing apurinic/apyrimidinic (known as abasic) sites, is also involved in the generation of small DNA fragments during DNA repair.
Voluntary running wheel exercise significantly increases levels of BDNF, activates CREB, and upregulates APE1 in the cerebral cortex and hippocampus of mice.
data provide new insight into error-prone repair of AID-induced lesions, which we propose is facilitated by down-regulation of APE1 and up-regulation of APE2 expression in germinal center B cells.
Transient OGG1, APE1, PARP1 and Polbeta expression in an Alzheimer's disease mouse model.
APE1 enhances in vivo vascular repair effects of endothelial progenitor cells in part through the maintenance of adhesion properties of EPCs during oxidative stress.
Apurinic/apyrimidinic (AP) sites occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. AP sites are pre-mutagenic lesions that can prevent normal DNA replication so the cell contains systems to identify and repair such sites. Class II AP endonucleases cleave the phosphodiester backbone 5' to the AP site. This gene encodes the major AP endonuclease in human cells. Splice variants have been found for this gene\; all encode the same protein.
DNA-(apurinic or apyrimidinic site) lyase
, APEX nuclease 1
, APEX nuclease (multifunctional DNA repair enzyme) 1
, AP endonuclease class I
, AP lyase
, apurinic-apyrimidinic endonuclease 1
, apurinic/apyrimidinic (abasic) endonuclease
, deoxyribonuclease (apurinic or apyrimidinic)
, protein REF-1
, redox factor-1
, AP endonuclease 1
, apurinic/apyrimidinic endonuclease 1
, apurinic/apyrimidinic endonuclease
, Apurinic-apyrimidinic endonuclease 1
, Redox factor-1
, APEX nuclease