Polyclonal Rabbit 53BP1 (Phospho-Ser25) Antibody
- Known as:
- Polyclonal Rabbit 53BP1 (Phospho-Ser25) Antibody
- Catalog number:
- KA0018
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit 53BP1 (Phospho-Ser25) Antibody
Related genes to: Polyclonal Rabbit 53BP1 (Phospho-Ser25) Antibody
- Gene:
- TP53BP1 NIH gene
- Name:
- tumor protein p53 binding protein 1
- Previous symbol:
- -
- Synonyms:
- 53BP1, p202, TDRD30
- Chromosome:
- 15q15.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-24
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal Rabbit 53BP1 (Phospho-Ser25) Antibody
Related articles to: Polyclonal Rabbit 53BP1 (Phospho-Ser25) Antibody
- Long non-coding RNAs (lncRNAs) are integral to the regulation of viral tumorigenesis. We have previously identified that the chicken lncRNA-803, which responds to Marek's disease virus (MDV), inhibits apoptosis in the chicken embryonic fibroblast cell line DF-1, accompanied by changes in the expression of the p53 protein. Nonetheless, the molecular mechanism of lncRNA-803 in apoptosis has yet to be elucidated. - Source: PubMed
Publication date: 2026/04/12
Han ShuoYang JingyiQiu YunqiaoZhao ShuangJiang YingxueHan LipingHan Limei - Older maternal age at first vaginal delivery, defined in some studies as ≥30 years old, confers a significant increased risk of pelvic organ prolapse. Age-related impairment of postpartum recovery of levator ani muscles may help explain this association; yet, little is known about the biomolecular changes that occur in the levator ani after vaginal delivery, or with aging. - Source: PubMed
Publication date: 2026/04/15
Swenson Carolyn WPouladi NimaZabriskie Hannah ABourrant Paul-EmileLi JianrongWilson Liam SDrummond Micah JLussier Yves A - BRAF, a serine/threonine kinase, functions as a key effector of the MAPK signaling cascade and regulates cell proliferation and survival. Oncogenic BRAF mutations disrupt MAPK pathway homeostasis, contributing significantly to cancer progression and pathogenesis. BRAF phosphorylation is pivotal for modulating downstream signaling events. In this study, we performed a comprehensive analysis of global human phosphoproteomic datasets to elucidate BRAF phosphorylation dynamics and associated regulatory networks. The systematic annotation identified BRAF phosphorylation in 912 qualitative profiles across 166 studies and 234 quantitative differential datasets from 73 studies, revealing 44 and 21 distinct phosphosites, respectively. Class I phosphosites with localization probability ≥75% or A-score > 13 were filtered. A fold-change threshold of ≥1.3 for upregulation and ≤ 0.76 for downregulation was applied. Particularly, six predominant phosphorylation sites, S446, S729, S151, T401, S365, and S447, were frequently observed. Further analysis of melanoma-melanoma-specific phosphoproteomic datasets and correlations with gene expression data from melanoma cell lines revealed several key co-regulated proteins associated with the predominant BRAF phosphosites, including STAT3, BAD, CDK16, ITPKB, NPM1, MDC1, CHEK2, PRKDC, EIF3A, TP53BP1, RB1, and CDK14. These co-regulated proteins highlight the integration of BRAF signaling with critical processes, such as cell cycle control, apoptosis, DNA damage response, and protein synthesis in melanoma. Our analysis suggests that targeting BRAF-interacting proteins may also modulate oncogenic signaling pathways and represent promising biomarkers for melanoma diagnosis and therapy. - Source: PubMed
Publication date: 2026/04/03
Dcunha LeonaEdakkad BhavanaJohn LevinShivamurthy Prathik BasthikoppaBera PritamDas DebodiptaRaju RajeshBalaya Rex Devasahayam ArokiaKanekar Saptami - Wiskott-Aldrich Syndrome (WAS), a rare X-linked disorder, features microthrombocytopenia, eczema, immunodeficiency, and elevated malignancy risk due to genomic instability. While prior studies noted DNA repair deficits, the kinetics of ionizing radiation-induced DSB repair in WAS patients remain unclear. This study aimed to characterize DSB repair dynamics and radiation sensitivity in WAS lymphocytes using γH2AX and 53BP1 markers. Lymphocytes from four WAS patients, their carrier mothers, and healthy controls were analyzed. Baseline DSBs were quantified in non-irradiated cells, and repair kinetics assessed post 2 Gy gamma irradiation over 24 h. Immunofluorescence staining for γH2AX (early DSB marker) and 53BP1 (repair facilitator) was performed at multiple time points, with foci quantified via confocal microscopy. Repair half-lives were calculated using exponential decay models. WAS patients exhibited 16-24 fold higher baseline γH2AX and 53BP1 foci than control (mean), indicating spontaneous genomic instability. Post-irradiation, DSB repair in WAS lymphocytes was significantly delayed, with the mean foci repair half-life (T½) in WAS patients being approximately 1.6-fold longer than that of the control (mean). At 24 h post-irradiation, WAS patients retained nearly twice the number of residual foci compared to healthy controls, while carrier mothers mirrored control repair efficiency. This study provides the first evidence of prolonged DSB repair kinetics in WAS patients, emphasising heightened radiosensitivity and genomic instability. These findings suggest tailored radiation strategies in WAS management, particularly for bone marrow transplantation or genotoxic therapies, to mitigate risks and optimize outcomes. - Source: PubMed
Publication date: 2026/03/16
Pathak Ranjana SChaurasia Rajesh KumarSapra Balvinder KaurGaikwad PallaviBargir UmairMadkaikar ManishaShirsath Kapil BGoel AnjanaBhat Nagesh NKhan Arshad - DNA double-strand breaks (DSBs), the most lethal DNA lesions, are repaired primarily by homologous recombination (HR) or nonhomologous end joining (NHEJ). Caffeine is known to inhibit HR by displacing Rad51 from single-stranded DNA, but its impact on NHEJ was unclear. Here, we show that caffeine inhibits NHEJ in a concentration-dependent manner using biochemical and cellular assays. Increased 53BP1 and γ-H2AX foci upon caffeine exposure indicate inhibition of chromosomal NHEJ, leading to accumulation of DSBs. γ-H2AX immunofluorescence, neutral comet, and TUNEL assays revealed persistent DNA breaks and reduced repair. Mechanistically, in silico, biophysical, and biochemical analyses demonstrate that caffeine directly binds to XRCC4, disrupting its interaction with DNA ligase IV and thereby inhibiting repair. Biolayer interferometry confirmed caffeine-XRCC4 binding, with mutation of Thr133 reducing caffeine affinity and impairing XRCC4 recruitment to γ-H2AX-marked DSBs. Disruption of the predicted caffeine interaction site in XRCC4 (T133A) partially restored end joining in the presence of caffeine. Clonogenic survival assays showed decreased survival after caffeine treatment, more prominently in wild-type than in ligase IV-deficient cells. Immunodepletion and reconstitution experiments confirmed that caffeine specifically targets the ligase IV/XRCC4 complex. Thus, caffeine suppresses NHEJ by directly inhibiting ligase IV/XRCC4-mediated DNA end joining. - Source: PubMed
Kumari SusmitaSathees DivyaRai Prashant KumarSahu Lipsa RaniRaghavan Sathees C