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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
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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
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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
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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
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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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Study identified that APEX1 rs2307486 variants conferred an increased risk of mercaptopurine-related early onset neutropenia in pediatric acute lymphoblastic leukemia.
The redox domain of APE1 is necessary for the active mode of stimulation of DNA glycosylases (OGG1, MPG, MBD4). APE1-catalyzed oligomerization along DNA induces helix distortions, which in turn enable conformational selection and stimulation of DNA glycosylases.
APE1 removes 3' mismatches and DNA damage by placing the 3' group within the intra-helical DNA cavity via a non-base flipping mechanism.
This study identified 2837 genes whose expression is significantly changed following APE1 knockdown in pancreatic ductal adenocarcinoma.
MCP- and CP-induced oxidative stress alters APE1-dependent BER-pathway and also mediates cell survival signalling mechanisms via APE1 regulation, thereby promoting lung cancer cell survival and proliferation.
Study uncovered a novel interaction between APE1 and PRDX1, which existed in both the nuclear and cytosolic fractions. The loss of APE1 interaction with PRDX1 promotes APE1 redox function to activate binding of the transcription factor NF-kappaB onto the promoter of IL-8 involved in cancer invasion and metastasis, resulting in its upregulation.
APE1 contributes to the protective effects of resveratrol against neonatal hypoxicischemic brain injuries, and suggest that DNA repair enzymes, including APE1, may be a unique strategy for neuroprotection against this disease.
Studied the association between single-nucleotide polymorphism of apurinic/apyrimidinic endonuclease 1 (APEX1) rs1760944 and risk of nasopharyngeal carcinoma in a Chinese population.
this study demonstrates a novel role of extracellular APE1 in IL-6-dependent cellular responses.
Our results showed that DNA base excision repair proteins APE-1 and XRCC-1 are overexpressed in tongue squamous cell carcinoma and that XRCC-1 is associated with better clinical staging and nodal status.
For the first time, this work identifies Ref-1 as a novel molecular effector in T-ALL and demonstrates that Ref-1 redox inhibition results in potent inhibition of leukemia T cells, including relapsed T-ALL. These data also support E3330 as a specific Ref-1 small-molecule inhibitor for leukemia
Apurinic/apyrimidinic endonuclease 1 is downregulated in Pleomorphic Adenomas of salivary gland and overexpressed in Carcinoma ex Pleomorphic Adenomas, the increased expression of this protein is associated with a more aggressive behavior in Carcinoma ex Pleomorphic Adenomas, which suggests that this protein may represent a prognostic biomarker in the studied Salivary Gland Tumors.
our study demonstrates that elevation of acetylation level of APE1 in tumor could be a novel mechanism by which cells handle the elevated levels of DNA damages in response to genotoxic stress and maintain sustained proliferation.
The chemotherapy-naive serum APE1 level, which correlated with its tissue level inversely associated with progression-free survival of platinum-containing doublet chemotherapy, whereas post-treatment serum APE1 level was inversely associated with overall survival.
HOGG1 Ser326Cys, APE1 Asp148Glu and XRCC1 Arg399Gln polymorphisms are correlated with the risk and clinicopathological features of PACG.
Through the characterization of the interactomes of APE1 with RNA and other proteins, we demonstrate here a role for APE1 in pri-miRNA processing and stability via association with the DROSHA-processing complex during genotoxic stress. We also show that endonuclease activity of APE1 is required for the processing of miR-221/222 in regulating expression of the tumor suppressor PTEN.
Co-localization of AP endonuclease (APE1) with poly(ADP-ribose) polymerase 1 (PARP1) on DNA was found capable of inducing 1D diffusion of otherwise nonmotile PARP1, while excess APE1 also facilitated the dissociation of DNA-bound PARP1.
the APEX1 Asp148Glu polymorphism might be important in stimulating the development of prostate cancer rather than its invasiveness in various populations, especially for Asians.
our data reinforce the concept that non-synonymous APE1 variants present in the human population may act as cancer susceptibility alleles
Data suggest that APE1 could be a potential target for NSCLC metastasis and AT101 is a potent inhibitor in further treatment of NSCLC patients.
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.
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.
Data indicate an association of ovarian stimulation with a downregulation of mRNAs encoding the base excision repair proteins APEX1 and POLB as well as the 5-methyl-CpG-binding domain protein MBD3 in individual morula embryos.
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