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Human APEX1 Protein expressed in Wheat germ - ABIN1345305
Zhao, Gao, Zhang, Wei, Liu, Deng: Bcl2 inhibits abasic site repair by down-regulating APE1 endonuclease activity. in The Journal of biological chemistry 2008
The redox domain of APE1 is necessary for the active mode of stimulation of DNA glycosylases (OGG1 (show OGG1 Proteins), MPG (show MPG Proteins), MBD4 (show MBD4 Proteins)). 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 (show CD46 Proteins)- 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 (show PRDX1 Proteins), which existed in both the nuclear and cytosolic fractions. The loss of APE1 interaction with PRDX1 (show PRDX1 Proteins) promotes APE1 redox function to activate binding of the transcription factor NF-kappaB (show NFKB1 Proteins) onto the promoter of IL-8 (show IL8 Proteins) 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 (show IL6 Proteins)-dependent cellular responses.
Our results showed that DNA base excision repair proteins APE-1 and XRCC-1 (show XRCC1 Proteins) are overexpressed in tongue squamous cell carcinoma and that XRCC-1 (show XRCC1 Proteins) 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
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 (show COL2A1 Proteins), 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 (show IL12A Proteins) and enhances Th1 (show HAND1 Proteins) responses.
Is closely associated with upregulation of the Ref1 (show THOC4 Proteins)/Nrf2 (show NFE2L2 Proteins) signalling pathway.
Results show the stimulatory effect of PARP-1 (show PARP1 Proteins) on APE1-dependent base excision repair (BER). PARP-1 (show PARP1 Proteins) and APE1 appear to have a functional interaction in BER since PARP-1 (show PARP1 Proteins) 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 Proteins) 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).
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