RALY antibody - N-terminal region (ARP34074_P050)
- Known as:
- RALY (anti-) - N-terminal region (ARP34074_P050)
- Catalog number:
- arp34074_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- RALY antibody - N-terminal region (ARP34074_P050)
Related genes to: RALY antibody - N-terminal region (ARP34074_P050)
- Gene:
- RALY NIH gene
- Name:
- RALY heterogeneous nuclear ribonucleoprotein
- Previous symbol:
- -
- Synonyms:
- P542, HNRPCL2
- Chromosome:
- 20q11.22
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-21
- Date modifiied:
- 2016-10-05
Related products to: RALY antibody - N-terminal region (ARP34074_P050)
Related articles to: RALY antibody - N-terminal region (ARP34074_P050)
- Eggshell quality is a critical trait in poultry production, as it directly influences economic outcomes. The genetic architecture underlying this trait remains poorly characterized. In this study, we conducted a genome-wide association study (GWAS) on Chinese Wenshang Barred chickens at 43 weeks of age to identify genomic loci and candidate genes associated with eggshell quality. This analysis revealed 87 significant SNPs and 14 candidate genes. Genes including , , , , and were associated with eggshell weight; , , , , and with eggshell thickness; and and with eggshell strength. Notably, three SNPs emerged as the most promising markers for eggshell quality, though their functional roles in laying hens require further investigation. This study advances our understanding of the genetic basis of eggshell quality and holds significant practical implications for improving this trait through targeted breeding strategies. - Source: PubMed
Publication date: 2026/07/11
Wang JieHan HaixiaLiu JieLei QiuxiaLiu WeiSun YanHao DanLi FuweiWang XinxiaCao DingguoZhao XinhuaZhou Yan - A rapid DNA damage response (DDR) and efficient DNA repair are essential for maintaining genome integrity. As a central apical kinase, ATM phosphorylates multiple downstream substrates to initiate DDR signaling and coordinate DNA repair following double-strand breaks (DSBs). However, the precise molecular mechanisms underlying ATM activation remain incompletely understood. Here, we identify the RNA-binding protein RALY as a critical regulator of ATM activation. We show that RALY directly interacts with and stabilizes the acetyltransferase Tip60, a key activator of ATM. Mechanistically, RALY competes with Tip60 for binding to the E3 ubiquitin ligase Mdm2, thereby inhibiting Mdm2-mediated ubiquitination and degradation of Tip60. Functionally, inhibition of RALY impairs ATM activation, compromises DNA repair capacity, and enhances radiosensitivity of cancer cells in a Tip60-dependent manner. Our findings uncover a previously unrecognized role of RALY in regulating ATM activation and indicate RALY as a potential therapeutic target for enhancing radiosensitivity in cancer. - Source: PubMed
Publication date: 2026/07/21
Yao BoZhao KailiangYu NingWang NingChang YinianLuo LinzhuWang FangMei Yide - The heterogeneous nuclear ribonucleoprotein-associated protein Raly plays a role in regulating cell proliferation and metabolism in eukaryotic nerve cells. However, the biological significance of Raly in oligodendrocyte lineage progression has not been previously explored. In this study, we found that Raly expression decreased during maturation of oligodendrocyte lineage cells. Knockdown of Raly in primary oligodendrocyte progenitor cells cultured in differentiation medium resulted in a significant increase in myelin-related proteins myelin basic protein and MAG. Furthermore, injection of an adenovirus expressing Raly shRNA into the subventricular zone of mice promoted oligodendrocyte progenitor cell differentiation, restored white matter integrity, and ameliorated cognitive deficits in the bilateral common carotid artery stenosis and senescence model. We further investigated the mechanism by which Raly regulates oligodendrocyte progenitor cell differentiation. Downregulation of Raly in primary oligodendrocyte progenitor cells led to increased mRNA and protein levels of Sox10, a pivotal player in oligodendrocyte development. The stability of Sox10 mRNA was unaffected by Raly downregulation, and RNA immunoprecipitation assays showed no binding between Raly and Sox10 mRNA. Dual luciferase and chromatin immunoprecipitation assays revealed that Raly downregulated the transcription of Sox10 by binding to a site located 1200 bp upstream of the Sox10 start codon. Collectively, our findings suggest that Raly plays a crucial role in oligodendrocyte progenitor cell differentiation and negatively regulates Sox10. These results may provide new insights into therapeutic strategies for neurological disorders associated with hypomyelination. - Source: PubMed
Publication date: 2026/06/20
Zhang ZhiShu XinSun LiangLi ChenggangGao ShenghanXia ShengnanShao PengfeiBao XinyuXu YuhaoXu Yun - The oncoprotein c-Myc is frequently dysregulated in human cancers, yet the underlying mechanisms remain elusive. Here, we identify the RNA-binding protein RALY as a critical post-translational stabilizer of c-Myc. RALY homodimerizes and acts as a scaffold to bridge the deubiquitinating enzyme USP22 to c-Myc, thereby preventing c-Myc ubiquitination and proteasomal degradation. Under physiological growth factor stimulation, RALY is phosphorylated by Akt at S106 and T160. This phosphorylation event enables ternary complex formation with USP22 and c-Myc, promoting c-Myc stabilization and driving RALY's oncogenic activity. Furthermore, a synthetic peptide derived from RALY, termed RAMi, disrupts the RALY-USP22-c-Myc complex, destabilizes c-Myc, and exhibits potent anti-tumor effects. Together, these findings reveal Akt-mediated RALY phosphorylation as a molecular switch governing c-Myc stability and underscore the therapeutic potential of targeting the RALY-USP22-c-Myc axis in cancer. - Source: PubMed
Publication date: 2026/05/29
Yu NingZhao KailiangWu XianningYao BoGuo XiaoruiTang SuyunHu HaoWang ZhongyuWang NingMei Yide - The RNA-binding protein RALY is an important member of the heterogeneous nuclear ribonucleoproteins (hnRNPs). It can target and regulate the key links of the RNA metabolic networks, such as RNA alternative splicing and stability maintenance, and is deeply involved in biological processes such as cell proliferation, metabolic reprogramming, and exosome biogenesis. RALY functions as a core regulator in tumorigenesis and tumor progression. In recent years, studies on RALY in cancer have been increasing. It is abnormally highly expressed in hepatocellular carcinoma, colorectal cancer, lung cancer, and other tumors. Emerging evidence suggests its oncogenic functions, multiple regulatory mechanisms, and potential clinical translational value, providing a candidate target for tumor precision therapy. At the mechanism level, RALY mainly plays a role in promoting cancer by regulating the three core methods of target gene alternative splicing, post-translational modifications (PTMs) of itself (ubiquitination, glycosylation, etc.), and mediating tumor metabolic reprogramming, thereby driving malignant biological behaviors such as tumor cell proliferation, invasion, metastasis, and chemotherapy resistance. At the clinical level, high RALY expression is associated with poor patient prognosis, indicating that it may serve as a promising candidate prognostic marker. This article reviews the molecular structure and core functions of RALY, focuses on its regulatory mechanisms and clinical significance in various tumors, and discusses the prospects and challenges of targeting RALY so as to provide theoretical support and direction for basic research and clinical translation of RALY-related tumors. - Source: PubMed
Publication date: 2026/04/22
Huang JialeJia LizhouLiu YuexinGao LingnaWeng ZhihuiLi Yanmei