MRE11A Antibody
- Known as:
- MRE11A Antibody
- Catalog number:
- csb-pa014786esr1hu
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- MRE11A Antibody
Related genes to: MRE11A Antibody
- Gene:
- MRE11 NIH gene
- Name:
- MRE11 homolog, double strand break repair nuclease
- Previous symbol:
- MRE11A
- Synonyms:
- ATLD
- Chromosome:
- 11q21
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-05
- Date modifiied:
- 2019-04-23
Related products to: MRE11A Antibody
Related articles to: MRE11A Antibody
- Protein lactylation plays a key role in cancer progression and chemotherapy sensitivity. Glycolysis inhibitors offer promise, particularly through combination strategies to counter metabolic compensation. - Source: PubMed
Publication date: 2026/08/05
Li CaifengCui ZhaoSun WenlongLiu WeiDeng ShiwenCao JunxianCao XuxiaWang XunChen PengYang Hongjun - Inflammation exerts context-dependent influences on tumor progression and therapeutic response. Although chemotherapy remains a cornerstone of cancer treatment, its functional interplay with inflammatory signaling is still incompletely understood. Here, we identify TANK-binding kinase 1 (TBK1) as a critical modulator of chemotherapeutic efficacy through its impact on DNA damage repair. TBK1 activation potentiates cancer-cell death induced by chemotherapeutic agents by promoting DNA damage and impairing homologous recombination (HR) repair. This effect occurs independently of canonical inflammatory cytokines, as demonstrated in IRF3- and p65- double deficient cells. Mechanistically, TBK1 suppresses recruitment of the key HR factor Meiotic Recombination 11 Homolog 1 (MRE11) to PARP1 at DNA-damage sites in a kinase-activity-dependent yet cytokine-independent manner. Furthermore, TBK1 activation correlates with enhanced p53 signaling and genomic instability, providing a molecular basis for its pro-death effects under chemotherapy. Collectively, these findings reveal a previously unrecognized function of TBK1 in modulating the DNA-damage response, linking inflammatory signaling to genome destabilization and identifying the TBK1-MRE11 axis as a potential target to enhance chemotherapeutic efficacy. - Source: PubMed
Publication date: 2026/08/14
Zhou WeiWang XiangyuSteigleder Susanne SXing AoweiYang DanLi ZhuoyueLiu HongjiZhang YuxinWang WenjingShen FeiyangTang YihanDeng LinJiang Hui - Against the backdrop of green biomanufacturing, engineering methanol-utilizing Komagataella phaffii (K. phaffii) represents an effective strategy to expand the one carbon (C1) product profile and speed up the industrialization of C1-based bioeconomy. To address the technical challenges of low efficiency and cumbersome experimental procedures for multiplex gene editing and precise large-fragment integration during the reconstruction of complex metabolic pathways in K. phaffii, this study established a CRISPR toolkit - Efficient Multi-Gene Editing System 3.0 (EMGES 3.0) - which enabled one-step large-fragment integration coupled with multiplex gene knockout. EMGES 3.0 was constructed through the synergistic optimization of a repair-engineered chassis and an episomal CRISPR vector. For chassis engineering, five DNA repair modules: Δlig4 (DNA Ligase IV, non-homologous end joining end ligation), ppMRE11(The endogenous MRE11 gene from Pichia pastoris) overexpression (The Meiotic Recombination 11, DNA double-strand break end resection), Δrad9 (Radiation-Sensitive 9, DNA damage checkpoint regulation), Δmph1 (Mutator Phenotype Helicase 1, improvement of homologous recombinant strand extension), and PapRecT-PaSSB co-expression (stabilization of recombination intermediates) were integrated to generate the highly recombinogenic strain Y09. For vector engineering, cenARS was replaced by panARS and the endogenous promoter P was employed to drive the double hammerhead ribozyme-single guide RNA-hepatitis delta virus ribozyme (double HH-sgRNA-HDV: dHgH)-mediated sgRNA expression, yielding the optimized vector Nov_pGAP_panARS_pLAT1_Cas9. These two features on K. phaffii together enhanced the EMGES 3.0 to a higher standard of transformation rate and editing efficiency. According to our results, EMGES 3.0 achieved dual-functional gene knockout efficiencies between 76.6% and 100%. For insertion of medium-long fragments (>4.5 kb), the efficiency achieved 93.3%. In addition, the one-step integration of ultra-long fragments (>16 kb) achieved 14.8%, which was reported for the first time. Furthermore, the efficiency of simultaneous long-fragment integration at three neutral loci reached 38.4% (>15 kb). We applied the system for one-step production of free fatty acids (FFAs, yield: 5.82 ∼ 7.30 mg/L/OD) and resveratrol (yield: 1.14 ∼ 1.28 mg/L) using methanol as the sole carbon source. EMGES 3.0 provides a robust technical foundation for complex compounds biosynthesis and high-yield industrial strains, while also advancing K. phaffii as an industrial synthetic biology chassis for efficient C1 utilization. - Source: PubMed
Publication date: 2026/08/13
Yu ZhixianChen KaidiMaimaitirexiati GulikeziBai ZhenminLi SongtaoYu AiqunYu TaoGuo Shuyuan - Homologous recombination repair (HRR) pathway defects are critical drivers of hereditary cancers, yet population-specific prevalence data from India remain limited. Current testing practices disproportionately focus on , potentially underidentifying patients with other HRR gene variants who could benefit from targeted therapies. - Source: PubMed
Publication date: 2026/08/13
Kapoor AkhilUthale SrushtiChain AnamikaRungta ArchiAnoop AnjanaGupta AnujSansar BipineshMishra Bal KrishnaPal AnkitaThakkar SoumyaSarin Rajiv - Replication stress threatens genome integrity by stalling replication forks, which may lead to double-stranded DNA (dsDNA) breaks. Stalled replication forks can be rescued through the fork reversal mechanism, yet they remain vulnerable to nucleolytic attack. Here, we identify nucleostemin (NS/GNL3) as a critical fork-stabilizing factor. We show that NS rapidly accumulates at hydroxyurea-stalled forks and is indispensable for protecting reversed forks, with NS depletion abolishing RAD51 foci formation and unleashing MRE11-mediated degradation. Through biochemical reconstitution and single-molecule fluorescence resonance energy transfer (FRET), we demonstrate that NS binds DNA directly, engages RAD51, and promotes nucleoprotein filament assembly on the dsDNA segment adjacent to the single-stranded DNA/dsDNA junction. This NS-RAD51 complex synergistically shields nascent strands from MRE11-mediated nucleolytic attack. Our work uncovers a new mechanism of fork protection and positions NS as a key guardian of genome integrity under replication stress. - Source: PubMed
Chang Chih-ChunTsai Siang-ShengChou Chang-LeChang Yi-HsuanHung Chia-TaiTsai Robert Y LLi Hung-WenLiaw HungjiunChi Peter