ASF1A Antibody
- Known as:
- ASF1A Antibody
- Catalog number:
- AF1119b
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- ASF1A Antibody
Related genes to: ASF1A Antibody
- Gene:
- ASF1A NIH gene
- Name:
- anti-silencing function 1A histone chaperone
- Previous symbol:
- -
- Synonyms:
- DKFZP547E2110, CIA
- Chromosome:
- 6q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-01
- Date modifiied:
- 2015-09-11
Related products to: ASF1A Antibody
Related articles to: ASF1A Antibody
- Psoriasis is a chronic, immune-mediated disorder with an unmet need for effective treatments. To systematically prioritize therapeutic targets, we integrated proteome-wide Mendelian randomization (MR) with expression validation in blood/skin, genetic susceptibility analysis, differential gene expression (DGE) from bulk and single-cell RNA sequencing (scRNA-seq), colocalization, pathway enrichment, and protein-protein interaction analyses. - Source: PubMed
Si ShuchengWang XiaoxiaoZhan Siyan - Histone chaperone ASF1B is largely known to be functionally correlated with cell proliferation and cell cycle. We found that the expression of ASF1B was abundant together with histone variant H3.3 during in mouse fetal liver cells. However, the mechanism underlying this coordination is still unclear. HIRA, a H3.3 specific chaperone, was dispensable in fetal hematopoiesis. In contrast, we found that ASF1B predominantly regulated H3.3 encoding genes and erythroid genes, whereas ASF1A served a compensatory function. Notably, ASF1B occupied >70% of H3.3 nucleosomes and determined H3.3 enrichment at erythroid gene promoters and enhancers. However, loss of ASF1B de-repressed the expression of embryonic/fetal globin genes by altering enrichment of H3.3 and erythroid transcription factors as well as chromatin accessibility. The regulatory pathway of ASF1B in H3.3 enrichment involved the recruitment of chromatin remodeler BRG1 and accumulation of H3K27ac in active chromatin. In summary, ASF1B plays a crucial role in enrichment of H3.3 nucleosomes and establishment of the chromatin environment to affect erythroid gene expression, highlighting the therapeutic potential of ASF1B in targeting erythrocyte disorders, such as β-globin hemoglobinopathies. - Source: PubMed
Liu JinleiSong XuemeiZhou LecongZhao YanguKim JuhyunLi JunDean AnnGuo Xiang - Amyotrophic lateral sclerosis (ALS) is characterised by the aggregation of TDP-43 and mutant FUS in the cytoplasm of affected motor neurons. Accumulation of DNA damage is emerging as a novel correlative trait of ALS. We recently showed that formation of TDP-43 and FUS cytoplasmic inclusions (CIs) lead to DNA damage accumulation through dysregulation of the DNA damage response (DDR). However, the multiple molecular mechanisms contributing to DNA damage accumulation in affected motor neurons in ALS have not been fully elucidated. In recent years, chemical inhibition of the serine/threonine kinase CHK1 was shown to lead to accumulation of DNA breaks as well as increased apoptosis, in differentiated cortical neurons. Notably, CHK1 has been involved in DNA double-strand break repair in non-dividing cells, by acting through the histone chaperone ASF1A. In this article, we show that cells bearing FUS and TDP-43 CIs show downregulation of the protein levels of CHK1 and ASF1A. We observe CHK1 protein downregulation in neuronal cell lines, as well as in patient-derived motor neurons progenitors and in the spinal cord of a FUS-ALS mouse model. Restoration of the nuclear levels of CHK1 and ASF1A via transient overexpression, is sufficient to reduce DNA damage signal accumulation and rescues DDR defects. Importantly, we show that the ubiquitin-proteasome pathway is responsible for CHK1 degradation in cells bearing FUS CI, since its inhibition restores CHK1 and ASF1A protein levels. Our study demonstrates that proteasomal-dependent CHK1 and ASF1A downregulation contributes to accumulation of DNA damage in cells affected by ALS-linked protein aggregates. - Source: PubMed
Publication date: 2026/05/06
Modafferi StefaniaSilenzi ValentinaGarbelli AnnaLazoi GloriaScarian EveljnD'Uva SaraSantini TizianaRiccardi AdelaideCozzolino MauroPansarasa OriettaD'Ambrosi NadiaSabbioneda SimoneMorlando MariangelaFrancia Sofia - Glioblastoma (GBM) is characterized by pronounced tumor heterogeneity and a complex immune microenvironment, contributing to poor patient survival outcomes. In this study, we comprehensively dissected the tumor microenvironment (TME) and uncovered potential molecular mechanisms by integrating single-cell, bulk, and spatial transcriptomic data. Hallmarks of malignancy and cell cycle regulatory pathways were consistently enriched across these modalities, promoting tumor cell proliferation and progression. Using a machine learning algorithm, we identified seven hallmark-related prognostic signatures (HMsig), namely AEBP1, ASF1A, PRPS1, DCC, OPHN1, IL13RA2, and HDAC5-whose predictive importance was validated through SHAP analysis. Ligand-receptor (LR) interaction analysis further revealed that interactions involving OPHN1 were associated with poorer prognosis. Along the pseudotime trajectory of T cell differentiation, immune checkpoint genes (ICGs) LAG3, PDCD1, and HAVCR2 were substantially upregulated. Notably, synergistic transcriptional regulation between tumor-related HMsig genes and ICGs in T cells was identified as a key factor influencing patient survival. Spatial transcriptomic analysis demonstrated the existence of synergistic gene interactions, deciphering the immunomodulatory functions of GBM biomarkers within the TME. - Source: PubMed
Li TengyueMi WanqiYan HuaruiMa YiningJiang HanYang XiaoxuZhang YunpengHu Congxue - Extrachromosomal DNAs (ecDNAs) play an important role in tumor progression. ecDNA hubs have been shown to be anchored by BRD4, a chromatin reader. However, the chromatin organization of ecDNA hub remains unknown. Here we show that histone 3 lysine 56 acetylation (H3K56ac) mark binds to BRD4 specifically. Knockdown of BRD4 decreased the ecDNA hub signals by the ecTag method. Knockdown of an epigenetic player (USP7), histone acetyltransferase (CBP), or histone chaperone (Asf1a) that regulates H3K56ac mark also decreased ecDNA hub signals and H3K56ac levels, supporting the role of H3K56ac in regulating ecDNA hub maintenance. Co-immunoprecipitation experiments showed the interactions of BRD4, USP7, Asf1a, and CBP. Analysis of ChIP-seq datasets showed that both H3K56ac and H3K27ac converged with BRD4 binding at the ecDNA-chromosome interaction sites and ecDNA itself. However, H3K56ac had a widespread enrichment with most BRD4-occupied sites compared with H3K27ac that occupied a limited subset of BRD4 peaks. These results present a framework of ecDNA hub chromatin organization that maintains ecDNA hub integrity, further providing therapeutic options that could be used to target ecDNA hubs. - Source: PubMed
Publication date: 2026/01/06
Liao Li-ZhuWu Chang-JiunChen Yu-AnLin Tzu-ChinLin Po-HungWei Chia-LinWu Kou-Juey