Polyclonal Rabbit APEX1 Antibody
- Known as:
- Polyclonal Rabbit APEX1 Antibody
- Catalog number:
- KA0241
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit APEX1 Antibody
Related genes to: Polyclonal Rabbit APEX1 Antibody
- Gene:
- APEX1 NIH gene
- Name:
- apurinic/apyrimidinic endodeoxyribonuclease 1
- Previous symbol:
- APEX
- Synonyms:
- APE, REF1, HAP1, APX, APEN, REF-1, APE-1
- Chromosome:
- 14q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-05-22
- Date modifiied:
- 2016-03-08
Related products to: Polyclonal Rabbit APEX1 Antibody
Related articles to: Polyclonal Rabbit APEX1 Antibody
- DNA oxidation damage and its repair are essential for maintaining genomic integrity in the human limbal epithelium, which harbors corneal epithelial stem cells. This study investigated the distribution of the DNA base oxidation 8-oxoguanine (8-oxoG) and the base excision repair (BER) enzymes 8-oxoguanine DNA glycosylase (OGG1) and apurinic/apyrimidinic endonuclease 1 (APE1) in non-cultured and eye-bank organ-cultured human limbal epithelia. Immunohistochemistry was used to assess the localization and staining intensity of 8-oxoG, OGG1, and APE1, evaluated semi-quantitatively and by image analysis. In situ hybridization was performed to detect the distribution of and gene expression in organ-cultured tissue. In non-cultured limbal epithelia, nuclear 8-oxoG staining was more frequently observed in superficial epithelial layers, whereas nuclear OGG1 and APE1 staining predominated in basal layers. In organ-cultured epithelia, a higher proportion of superficial nuclei exhibited 8-oxoG staining, while the basal predominance of OGG1 was reduced and that of APE1 was preserved. Transcripts of and were detected in basal- as well as in suprabasal layers of organ-cultured epithelia. These findings demonstrate the presence of DNA base oxidation and BER-related enzymes in basal and suprabasal human limbal epithelial cells during storage of corneal tissue under commonly used eye-bank organ-cultured conditions prior to transplantation. - Source: PubMed
Publication date: 2026/06/04
Nicolaissen Bjørn OttoNguyen GiangBeraki KahsaiAzqueta AmayaPetrovski GoranMoe Morten CKrohn-Hansen DagCollins Andrew RNicolaissen BjørnLorenzo Yolanda - Apurinic/apyrimidinic (AP) sites are among the most frequent DNA lesions, arising thousands of times per cell each day. These lesions threaten genomic stability and, if left unrepaired, can lead to mutagenesis and disease. The base excision repair enzyme Apurinic/Apyrimidinic Endonuclease I (APE1) initiates repair by cleaving DNA at AP-sites, yet how APE1 efficiently identifies these lesions within vast excesses of undamaged DNA has remained unclear. Using single-molecule imaging, we show that APE1 employs a dynamic search strategy that integrates one-dimensional (1D) and three-dimensional (3D) diffusion to rapidly scan DNA. On non-damaged DNA, APE1 undergoes rapid diffusion, enabling efficient interrogation of large genomic regions within a single binding event. Upon encountering an AP-site, APE1 transitions from a mobile search state to a stable lesion-bound complex that remains localized at the site of damage. Experiments with APE1 variants further reveal that the intrinsically disordered N-terminal domain promotes 1D diffusion, residue R177 stabilizes APE1 at the AP-site after recognition, and catalytic residues D210 and E96 facilitate enzyme release following cleavage. Together, these findings define how APE1 balances rapid genome surveillance with stable lesion engagement and timely release. More broadly, this work provides a mechanistic framework for how DNA repair enzymes efficiently locate and process rare lesions embedded within excess undamaged DNA. - Source: PubMed
DeHart Kaitlin MOden Peyton NWeaver Tyler MSchaich Matthew AVan Houten BennettFreudenthal Bret D - Studies have shown that mitochondrial dysfunction in macrophages worsens inflammation and impedes repair after acute myocardial infarction (AMI). This study aimed to identify and validate biomarkers of AMI associated with mitochondria-related genes (MRGs) and macrophage polarization-related genes (MPRGs), offering new targets and strategies for therapeutic intervention of AMI. - Source: PubMed
Publication date: 2026/05/29
Qu NanBai FawenLan Jin - Extracellular vesicles (EVs) are stably present in body fluids and carry diverse molecular cargos, including proteins and nucleic acids, making them an ideal information carrier for liquid biopsy. However, most existing EV assays focus on a single class of markers, and combining multiple markers within the same class often introduces informational redundancy, thereby limiting diagnostic performance. To address this challenge, we developed a one-pot dual-biomarker detection platform driven by an AND logic gate, inspired by the enrichment of the endonuclease APE1 and tumor-associated miRNAs in cancer-related EVs. In our platform, low-abundance target miRNA was first efficiently converted into abundant product probes (Pp) via strand displacement amplification (SDA). The resulting Pp then hybridized with an AP-site containing signal probe to form a cleavage-competent substrate, which was catalytically cleaved by APE1 to restore fluorescence. Meanwhile, the released Pp can repeatedly initiate additional cleavage cycles, enabling cascading signal amplification. The platform achieved a limit of detection of 8 fM for miRNA and 0.008 U/mL for APE1. In plasma EVs from gastric cancer patients and healthy donors, the AND-gated dual-marker readout yields an area under the ROC curve (AUC) of 0.957, significantly outperforming single-marker RT-qPCR miRNA analysis (AUC = 0.823), indicating improved discrimination in clinical samples. Overall, our work provided a simple synergistic logic-gated framework for integrating multi-class EV biomarkers, with potential applications in early cancer screening and dynamic disease monitoring. - Source: PubMed
Publication date: 2026/05/26
Ge KeYe Kai - Efficient recognition of DNA lesions such as apurinic/apyrimidinic (AP) sites is essential for maintaining genome stability. Apurinic/apyrimidinic endonuclease 1 (APE1) is the primary eukaryotic AP endonuclease, yet how it identifies rare lesions among vast stretches of undamaged DNA remains incompletely understood. Using single-molecule imaging combined with molecular dynamics simulations, we reveal that APE1 employs a distinctive dual mechanism to search DNA damage. First, Mg2+ coordination at the active site neutralizes clustered negative charges, stabilizing electrostatic contacts during scanning. Second, its N-terminal intrinsically disordered region (IDR)-a feature conserved only in eukaryotic homologs but absent in prokaryotic ExoIII-not only interacts with DNA through transient IDR contacts but also engages continuous interactions via the unprecedented Arg177 residue within the structured nuclease domain, thereby prolonging residence time and enabling long-range diffusion. Together, these two modules synergize to promote a sliding-based search strategy tailored to the complexity of eukaryotic genomes. Consistent with this model, IDR deletion restricts APE1 to 3D collisions, whereas IDR duplication enhances 1D scanning. Thus, APE1 exemplifies how structural disorder and metal-ion coordination integrate to enable long-range lesion recognition, highlighting an evolutionary innovation in eukaryotic DNA repair. - Source: PubMed
Lee DonghunKim SubinJo GyeongpilKim JuwonYoo JungminYoo JejoongLee Ja YilLee Gwangrog