HNRNPA0 Antibody (AMM10005)
- Known as:
- HNRNPA0 Antibody (AMM10005)
- Catalog number:
- amm10005
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- HNRNPA0 Antibody (AMM10005)
Related genes to: HNRNPA0 Antibody (AMM10005)
- Gene:
- HNRNPA0 NIH gene
- Name:
- heterogeneous nuclear ribonucleoprotein A0
- Previous symbol:
- HNRPA0
- Synonyms:
- hnRNPA0
- Chromosome:
- 5q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-28
- Date modifiied:
- 2016-10-05
Related products to: HNRNPA0 Antibody (AMM10005)
Related articles to: HNRNPA0 Antibody (AMM10005)
- RNA guanine quadruplexes (rG4s) are noncanonical nucleic acid structures that contribute to diverse cellular functions and disease mechanisms. Defining the proteins that interact with rG4s (rG4IPs) is essential for elucidating their biological roles. Here, we build on the RNA-protein interaction detection (RaPID) platform to develop G4-RaPID, a tailored chemoproteomic strategy for the unbiased profiling of rG4IPs in living cells. Using G4-RaPID, we identified 105 candidate rG4IPs that were commonly enriched across three distinct rG4 sequences. Biochemical analyses confirmed that recombinant hnRNPA0, CHD4, and IGF2BP1 proteins directly bind rG4 structures . In addition, CLIP-seq experiments revealed significant enrichment of hnRNPA0 binding at endogenous rG4 loci. Luciferase reporter assays further demonstrated that hnRNPA0 engages the rG4 in the 5' UTR of mRNA to negatively regulate its translation. Together, these results establish G4-RaPID as a robust approach for mapping rG4-protein interactions in living cells and document hnRNPA0-rG4 recognition as a regulatory mechanism controlling mRNA translation. - Source: PubMed
Publication date: 2026/04/17
Tang FengLiang XiaochenPorter Douglas FMiao WeiliMaehlmann KevinYuan JunKhavari Paul AWang Yinsheng - Influenza B virus (IBV) is a type of influenza virus. The NS1 protein is a powerful regulatory factor during the process of viral infection of host cells and plays an important role in viral replication, virulence, and innate immunity. Protein-protein interactions play an extremely important role throughout the entire life cycle of viral infection of host cells. Identifying host proteins that interact with IBV NS1 protein is of great significance for exploring the pathogenic mechanism of IBV and screening for new antiviral drugs. In this study, the NS1 protein was purified by immobilized metal affinity chromatography (IMAC) using nickel-charged resin and the known host interactome of IBV NS1 was expanded using Pull-down combined with mass spectrometry (LC-MS/MS). Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG), and Protein-Protein Interaction (PPI) analyses were conducted on the candidate-interacting proteins identified in the mass spectrometry results. These identified candidate-interacting proteins are mainly involved in biological processes such as protein translation, protein folding, mRNA processing, small molecule metabolism, ribosome biogenesis, and viral processes. The heterogeneous nuclear ribonucleoprotein (hnRNPA0) and the DDX39B protein of the DEAD-box RNA helicase family were further studied. Co-IP, IFA, and BiFC all confirmed that the NS1 protein of IBV interacts with the hnRNPA0 and the DDX39B proteins. We further mapped the interaction between the NS1-RBD and NS1-ED domains of NS1 protein and the hnRNPA0-GRD domain. These data provide resources for further research on the mechanism by which NS1 protein modulates host cells. - Source: PubMed
Publication date: 2026/03/12
Zhang BeibeiWang HailiWang YanweiLiu XiaoYan WenyingZhou JingmingZhang LeiLiu YankaiChen YumeiLiang ChaoWang Aiping - Esophageal squamous cell carcinoma (ESCC) remains a leading cause of cancer-related mortality worldwide. Long non-coding RNAs (lncRNAs) play essential roles in ESCC progression. In this study, we profiled lncRNA expression in ESCC cells following serum deprivation and identified LHFPL3-AS2 as a serum starvation-inducible, oncogenic lncRNA. LHFPL3-AS2 could promote invasion and metastasis of ESCC cells in vitro and in vivo. Mechanistically, LHFPL3-AS2 directly binds to hnRNPA0 protein, enhances its interaction with its kinase MAPKAP-K2 (MK2), and promotes MK2-mediated phosphorylation of hnRNPA0 at serine 84. The phosphorylated hnRNPA0 binds to several oncogenic transcripts, such as the BMP7 mRNAs, stabilizes these mRNAs and elevates their expression in ESCC cells. Importantly, LHFPL3-AS2 enhances polarization of macrophages toward an immunosuppressive M2 phenotype via upregulating BMP7 secretion by cancer cells, thereby facilitating tumor immune evasion and ESCC progression. Overall, our study identified a previously unappreciated LHFPL3-AS2-MK2-hnRNPA0-BMP7 axis in cancer progression under serum starvation conditions and provides mechanistic insight for ESCC. - Source: PubMed
Publication date: 2026/02/16
Xu YuanZhang ZiqiYang YantingLi MinxinWang HaipengZhang LongWang ShouyuRen ChuanliZhang NashaLi ZengjunYang Ming - MicroRNAs (miRNAs), a class of non-coding small RNAs, play critical roles in regulating adipocyte biology, including differentiation, proliferation, and lipid metabolism. This study investigates the role of miR-424-3p in adipogenesis. MiR-424-3p expression is dynamically upregulated during adipocyte differentiation. Functional analyses demonstrate that miR-424-3p overexpression suppresses lipid droplet accumulation and coordinately inhibits both anabolic (PPARγ, C/EBPα) and catabolic (ATGL, HSL) pathways; these effects are reversed by co-treatment with a miR-424-3p inhibitor. Lipidomic analysis reveals that miR-424-3p mediates membrane phospholipid remodeling, with significant changes predominantly in glycerophospholipids and sphingolipids, among which PE, PC, and LPE are the major affected species. Together with pathway enrichment analysis, increased lipid reactive oxygen species (ROS) levels, decreased glutathione (GSH) levels, and unaltered cell viability, these results collectively indicate that miR-424-3p may trigger ferroptosis signaling. Mechanistically, we demonstrate that miR-424-3p targets HNRNPA0, thereby upregulating p53 and suppressing ferroptosis inhibitors (SLC7A11, GPX4). HNRNPA0 overexpression reverses these phenotypes, restoring adipocyte metabolism and lipid storage capacity. Our findings establish miR-424-3p as an epigenetic regulator of adipose homeostasis via the HNRNPA0-p53-ferroptosis axis, which constrains lipid accumulation in 3T3-L1 cells. The evolutionary conservation of this mechanism across lipogenically active species highlights its potential as a therapeutic target for obesity-related metabolic disorders. - Source: PubMed
Publication date: 2025/12/09
Li MengYe YuqiLin ShashaJiang HanchenZhang DaweiZhang Jin - Venous thromboembolism (VTE) and chronic kidney disease (CKD) are multifactorial disorders characterized by complex genetic and molecular mechanisms. However, their shared genetic signatures and potential interrelations remain poorly understood. This study aimed to identify key genes and molecular pathways linking VTE and CKD through comprehensive transcriptomic and machine learning analyses. - Source: PubMed
Publication date: 2025/10/22
Li HuiLin CaiKuang Junjie