YBX1 antibody - middle region (ARP34396_P050)
- Known as:
- YBX1 (anti-) - middle region (ARP34396_P050)
- Catalog number:
- arp34396_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- YBX1 antibody - middle region (ARP34396_P050)
Related genes to: YBX1 antibody - middle region (ARP34396_P050)
- Gene:
- YBX1 NIH gene
- Name:
- Y-box binding protein 1
- Previous symbol:
- NSEP1
- Synonyms:
- YB-1, YB1, DBPB, NSEP-1, MDR-NF1, BP-8, CSDB, CSDA2
- Chromosome:
- 1p34.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-10-20
- Date modifiied:
- 2016-10-05
Related products to: YBX1 antibody - middle region (ARP34396_P050)
Related articles to: YBX1 antibody - middle region (ARP34396_P050)
- Porcine circovirus type 2 (PCV2), a major causative agent of PCV2-associated diseases, poses a serious threat to the global swine industry. The stability of PCV2 capsid (Cap) protein is critical for viral replication; however, the underlying mechanisms regulating Cap stability during PCV2 infection remain poorly understood. In this study, co-immunoprecipitation assays were used to demonstrate that PCV2 Cap protein can maintain its own stability by binding to the cellular Y-box-binding protein 1 (YBX1) during viral infection. Furthermore, binding domain mapping experiments revealed two specific regions essential for this interaction: the N-terminal arginine-rich motif (ARM) of PCV2 Cap (amino acid sequence: MTYPRRRYRRRRHRPRSHLG) and the amino acid residues RRRR within the C-terminal domain (CTD) of YBX1. Virus rescue experiments further confirmed that substituting all arginine residues with alanine in the N-terminal ARM of Cap completely abolished its binding to YBX1. Analysis of viral replication capacity showed that YBX1 promotes PCV2 replication by stabilizing the viral Cap protein. Additionally, knockdown of YBX1 significantly reduced the protein levels of PCV2 Cap, and this effect was reversed either by treatment with the proteasome inhibitor MG132 or by restoring YBX1 expression. Collectively, these findings demonstrate that YBX1 promotes PCV2 replication by directly interacting with the ARM of PCV2 Cap, thereby inhibiting the proteasomal degradation of Cap during viral infection. - Source: PubMed
Publication date: 2026/08/12
Zhou JianweiZhang QianqianDong XueGao WeiLan XiaoyuanZhou BeiyiQiu YonghuiXu WeiyinHui PengZeng PenghuiWang DedongHou LeiLiu Jue - - Source: PubMed
Publication date: 2026/08/10
Su HongboFan GuanzhiHuang JinQiu Xueshan - Colorectal cancer (CRC) is still a deadly malignancy all over the world. Previous studies have indicated that exosomes could remodel the microenvironment and promote tumor development. Furthermore, Galectin 3 (also known as LGALS3) was found to be present within the lumen of exosomes and participate in tumor progression. However, the effects of exosomal LGALS3 on CRC progression are still unclear. The advanced CRC cellular heterogeneity was identified in GSM7349819 database using scRNA-Seq analysis. Through the analysis of GSM7349819 database, transcriptome GSE159112 database, and GeneCards database, potential targets of lipid metabolism-related differential expression genes (DEGs) in macrophages and stem cells during CRC progression were identified. LGALS3 and Y-box binding protein 1 (YBX1) expression was determined using real-time quantitative polymerase chain reaction (RT-qPCR) and western blot. M2 polarization of macrophages was determined by measuring the M2-specific cell surface markers and cytokines. Binding between LGALS3 and YBX1 was analyzed using m5C RIP, RIP, and dual-luciferase reporter assays. PMA-treated THP1 cells were exposed to IL-4 and IL-13, generating M2-TAMs (THP1-M2). Effects of M2-TAM-derived exosomal YBX1 and LGALS3 on CRC development were assessed. Cell proliferation, invasion, sphere formation ability, and apoptosis were determined using EdU, Transwell, sphere formation, and flow cytometry. Oil Red O staining was applied for lipid accumulation. Role of M2-TAM-derived exosomal YBX1 on CRC tumor growth was determined in vivo experiments. Public database analysis exhibited that lipid metabolism-related gene LGALS3 was upregulated in CRC stem cells and M2 macrophages. Compared with THP1-M0, LGALS3 was increased in THP1-M2. LGALS3 was transferred from M2 TAMs to CRC cells via exosomes. M2 TAM-derived exosomal LGALS3 knockdown repressed CRC cell proliferation, invasion, stemness, lipid metabolism, promoted apoptosis, and inhibited tumor growth in vivo. Mechanistically, YBX1 recognized m5C modifications in LGALS3 mRNA and maintained mRNA stability in M2 TAM. YBX1-mediated m5C modification of exosomal LGALS3 derived from M2 TAM could promote CRC cell growth and lipid metabolism, providing a highly potential target for CRC. - Source: PubMed
Publication date: 2026/08/03
Yang LuZhang XiaolingMeng TaoDong DaiyuanFang XiangjieLi SujuanChang Tingmin - Syndecan binding protein (SDCBP) has been shown to be upregulated in esophageal squamous cell carcinoma (ESCC) and predicts poor prognosis in our previous research. SDCBP stimulated the proliferation and tumor formation and may be a target for ESCC. However, the participation of SDCBP in epithelial-mesenchymal transition (EMT) and ESCC metastasis is unclear. In this study, we found that SDCBP promoted the EMT process of ESCC cells and facilitated ESCC metastasis both in vitro and in vivo. Mechanically, SDCBP was found to influence the activation of the Wnt-β-catenin pathway. β-catenin expression and nuclear localization were regulated by SDCBP, accompanied by altered expression of Wnt-β-catenin pathway target genes. Additionally, SDCBP interacted with Y-box binding protein 1 (YBX1) and abnormally upregulated YBX1 in ESCC was responsible for SDCBP-mediated regulation of ESCC migration and invasion. Finally, SDCBP was identified to be transcriptionally regulated by the Wnt-β-catenin pathway. Thus, our study provides a better understanding of the SDCBP-YBX1-Wnt-β-catenin axis in ESCC metastasis and explores a positive feedback loop between SDCBP and the Wnt-β-catenin pathway, offering more compelling evidence for employing SDCBP as a target for ESCC treatment. - Source: PubMed
Du RuijuanBian BoLuo ManyuYuan ChenGuo KeleiLi KaiZhang HuiZhang GuangjiHan Li - This study investigates the epigenetic regulation of venous thromboembolism (VTE) in lung cancer (LC), focusing on the role of the crotonylation enzyme males absent on the first (MOF). Utilizing bulk RNA sequencing (RNA-seq) and bioinformatics analysis of clinical LC-VTE samples, we identified MOF as a significantly upregulated protein modification-related gene. Further mechanistic exploration revealed that MOF was associated with histone H3K18 crotonylation (H3K18cr) and increased transcriptional expression of Y-box binding protein 1 (YBX1). YBX1 enhanced the stability of Mucosa-associated Lymphoid Tissue Lymphoma Translocation Protein 1 (MALT1) mRNA, leading to increased MALT1 expression. MALT1 subsequently activated the NF-kappaB signaling pathway, where the subunit RELA directly bound to and upregulated the transcription of plasminogen activator inhibitor-1 (PAI-1). Elevated PAI-1 secretion by tumor cells drove a pro-coagulant state, ultimately contributing to VTE in LC patients. Both in vitro and in vivo models supported the involvement of the MOF/YBX1/MALT1/NF-kappaB/PAI-1 signaling axis. These findings suggest that MOF may promote LC-associated VTE possibly through histone crotonylation, thereby possibly linking histone crotonylation to hypercoagulability in LC. - Source: PubMed
Publication date: 2026/07/21
Liu YanYu FengJiang Jiuyang