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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 79 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 58 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
Show all 4 Pubmed References
Arabidopsis thaliana Polyclonal APEX1 Primary Antibody for WB - ABIN334581
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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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 (show XRCC1 Antibodies) 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 (show PARP1 Antibodies)) on DNA was found capable of inducing 1D diffusion of otherwise nonmotile PARP1 (show PARP1 Antibodies), while excess APE1 also facilitated the dissociation of DNA-bound PARP1 (show PARP1 Antibodies).
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.
Our findings suggest that constitutive overexpression of APE1 in esophageal adenocarcinoma may be an adaptive pro-survival mechanism that protects against the genotoxic lethal effects of bile reflux episodes.
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.
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 (show IL12A Antibodies) and enhances Th1 (show HAND1 Antibodies) responses.
Is closely associated with upregulation of the Ref1 (show THOC4 Antibodies)/Nrf2 (show NFE2L2 Antibodies) signalling pathway.
Results show the stimulatory effect of PARP-1 (show PARP1 Antibodies) on APE1-dependent base excision repair (BER). PARP-1 (show PARP1 Antibodies) and APE1 appear to have a functional interaction in BER since PARP-1 (show PARP1 Antibodies) 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 (show OGG1 Antibodies) 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 (show SCARA3 Antibodies)).
These results suggest that mitochondrial APE1/Ref-1 is contributed to the protective role to protein kinase C (show PKC Antibodies)-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.
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