APEX1 purified MaxPab Mouse Polyclonal Antibody
- Known as:
- APEX1 enriched MaxPab Mouse Polyclonal Antibody
- Catalog number:
- APO-000328-B01P
- Product Quantity:
- 0.05mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- APEX1 purified MaxPab Mouse Polyclonal Antibody
Related genes to: APEX1 purified MaxPab Mouse Polyclonal 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: APEX1 purified MaxPab Mouse Polyclonal Antibody
Related articles to: APEX1 purified MaxPab Mouse Polyclonal Antibody
- 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 - Accumulation of DNA damage, particularly oxidative DNA damage, is a major molecular driver of senescence and aging. The enzyme apurinic/apyrimidinic endonuclease-1 (Apex1) is essential for base-excision repair, but its role in protecting the brain from age-related deterioration remains unclear. Here we show that conditional knockout (cKO) of Apex1 in forebrain neurons causes early and progressive cognitive impairment in mice. Apex1 cKO mice display deficits in spatial learning and memory (8-12 weeks), alongside reduced synaptic proteins, altered neuronal morphology, and impaired long-term potentiation at 48 weeks. We further show that a 30% caloric restriction (CR) regimen at 8-48 weeks markedly attenuates these premature aging features and improves cognitive outcomes in Apex1 cKO mice. These findings confirm Apex1 as a critical genomic maintenance factor in the aging brain and highlight the Apex1 cKO model as a valuable tool for studying endogenous defenses and dietary interventions against aging. - Source: PubMed
Publication date: 2026/05/08
Wei Chris ZShi YejieZhang WentingHassan Sulaiman HShi RuyuPu HongjianMu HongfengAnne Stetler RLeak Rehana KChen Jun - Apurinic/apyrimidinic endonuclease 1 (APE1) is a multifunctional protein that occupies a key position at the interface between base excision repair (BER) and cellular redox control during inflammation. As the major AP endonuclease in the BER pathway, APE1 maintains the genomic stability by the repairing oxidative DNA lesions that accumulate in chronically inflamed tissues. In addition, its redox effector factor 1 (Ref-1) activity modulates a broad range of transcription factors, thereby influencing inflammatory cytokine production and the cellular response to redox imbalance. Through this combination of DNA repair and redox-signaling functions, APE1 acts as a central hub that couples oxidative DNA damage to inflammatory signaling networks. Dysregulation of APE1 expression or subcellular distribution has been associated with various inflammation-associated diseases, reflecting its broad impact on inflammatory pathology. This review summarizes current understanding of APE1's dual role in inflammation, highlights opportunities and challenges for therapeutic targeting, and discusses its emerging value in the precision monitoring and management of inflammation‑associated diseases. - Source: PubMed
Publication date: 2026/05/07
Xu PeilanZhou PengLuo JiaLiu YunXiao HeDu JiaLi MengxiaChen Chuan - Accurate cancer subtyping is essential for personalized medicine, yet existing diagnostic methods lack the multiplexing capability to decode complex biomarker signatures. Herein, we report a modular and dynamic DNA nanodevice, termed ichromatically outed herarchically responsie DNA ncoder (DRIVE), that enables the high-resolution molecular subtyping of triple-negative breast cancer (TNBC). Specifically, DRIVE integrates a tetrahedral DNA scaffold that is functionalized with two pairs of recognition and output modules responsive to apurinic/apyrimidinic endonuclease 1 (APE1) activity and specific microRNA (miRNA) expression. In the presence of APE1 and miRNA-21 (which are widely recognized as breast cancer biomarkers), the orthogonal recognition initiates a catalytic hairpin assembly (CHA) reaction that links a single DRIVE into a linear DNA nanostructure, thus significantly amplifying a monochromatic FAM signal. In TNBC subtypes that are characterized by the coexpression of APE1, miRNA-21, and miRNA-210, the cross-CHA makes a single DRIVE-form network DNA nanostructure, achieving the dichromatic FAM/Cy5 signal output. It is demonstrated that an approximately 4-fold enhancement in reaction kinetics of DRIVE is observed in comparison with that of individually dispersed probes. The dual-signal output enables a statistically significant differentiation of TNBC cells from other breast cancer subtypes. Together, this advance facilitates precise TNBC subtyping and provides great potential for accurate cancer diagnostics and personalized therapeutic strategies. - Source: PubMed
Publication date: 2026/05/03
Chen Zhao-PengWang Lu-XiZhou Xue-MeiLuo Xin-YuLei Yan-MeiZhuo Ying - Multivalent molecular interactions enhance binding affinity and enable functional regulation in biological systems, inspiring the development of multivalent materials for biosensing and biomedical applications. The capacity to reversibly switch between low-valency and multivalency as needed is key to regulating their function. However, current design strategies face challenges in enabling such switching within the same system through a response to multiple stimuli. Here, as a proof of concept, we demonstrate a switchable multivalent system for regulating thrombin activity. This system is based on thrombin aptamer-decorated DNA tile assembly and introduces stimuli-responsive plug-and-play modules that serve as dynamic, reversible, and orthogonal switches responding to the corresponding stimuli, including UV light, APE1, and RNase H. We construct three-layer switching cascades activated by one-, two-, or three stimuli to regulate thrombin activity. Building upon this programmable multivalent aptamer system, we further translate switchable modules into spatiotemporal control logic to construct a tristate circuit. We hope that the switchable DNA scaffold-based multivalent regulatory approach can provide a versatile modular platform with potential applications in precision medicine, biosensing, and biomaterials. - Source: PubMed
Publication date: 2026/04/30
Xu KaiqiZhao JiHu GuangShao LimingSong JieTang Linlin