PEA3 _ HIP EMSA Probe Set
- Known as:
- PEA3 _ HIP EMSA Probe Set
- Catalog number:
- AY1228P
- Product Quantity:
- 25 rxn
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- PEA3 _ HIP EMSA Probe Set
Related genes to: PEA3 _ HIP EMSA Probe Set
- Gene:
- ETV4 NIH gene
- Name:
- ETS variant 4
- Previous symbol:
- -
- Synonyms:
- E1A-F, E1AF, PEA3
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1995-03-27
- Date modifiied:
- 2016-02-25
Related products to: PEA3 _ HIP EMSA Probe Set
(+) Control probe (DNA), biotinylated(+) Control probe (RNA), biotinylated(-) Control probe (DNA), biotinylated(-) Control probe (RNA), biotinylated0.2 mm, 30 cm Spacer Set
0.2 mm, 30 cm Spacer Set0.35 mm, 30 cm Spacer Set
0.35 mm, 30 cm Spacer Set0.5 mm, 30 cm Spacer Set
0.5 mm, 30 cm Spacer Set0.75 mm Dual Gel Cast Set
0.75 mm Dual Gel Cast Set0.75 mm Plate Set, RM
0.75 mm Plate Set, RM
0.75 mm Plate Set, RM
Related articles to: PEA3 _ HIP EMSA Probe Set
- Transcriptional dysregulation in cancer is accompanied by an anabolic transcriptional response driving proliferation and metabolic adaptation. We previously found that oncogenic ETS variant transcription factor 4 (ETV4) overexpression is associated with DNA replication, glycolytic metabolism, tumor progression, and poor prognosis in non-small cell lung cancer (NSCLC). ETV4 is markedly overexpressed in multiple NSCLC datasets, including TCGA-LUAD and TCGA-LUSC. Importantly, ETV4 expression positively correlates with ubiquitin-specific protease 7 (USP7) and mitogen-activated protein kinase 7 (MAPK7) levels. While the E3 ligase constitutive photomorphogenesis protein 1 (COP1) is known to regulate ETV4 ubiquitination and degradation, ETV4 deubiquitination remains unclear. Our study reveals that USP7 deubiquitinates ETV4 and protects it from K11- and K48-linked ubiquitination and proteasomal degradation in NSCLC cells. ETV4 transcriptionally controls the expression of the MAPK pathway key gene MAPK7, which encodes extracellular signal-regulated kinase 5 (ERK5), and participates in the regulation of cell proliferation. Genetic knockdown or pharmacological inhibition of USP7 affects the transcriptional activity of ETV4 on its target gene MAPK7/ERK5. USP7 inhibitor P22077 significantly attenuates ETV4-MAPK7-induced cell proliferation in vitro and tumor growth in vivo. Furthermore, elevated ETV4, USP7, and ERK5 protein expressions are associated with poor prognosis of NSCLC patients. These findings identify that USP7 regulates the deubiquitination, stability, and transcriptional activity of ETV4, contributing to the malignant phenotype of ETV4. Inhibition of USP7 might be a promising target in NSCLC with the dysregulation of ETV4 or hyperactivated MAPK signaling. - Source: PubMed
Publication date: 2026/05/06
Meng XueZhang JiaxiZhang NingHou YuqiLi YimengKang JiaLi RuxinShi YinghuiWang JuanCheng LixinXing Lingxiao - The SMARCA4 gene encodes a key ATPase subunit of the SWI/SNF (BAF) chromatin-remodeling complex, which plays an essential role in regulating transcription and cellular differentiation. Loss-of-function alterations of SMARCA4 are common in various human cancers, including sarcomas; however, rare SMARCA4 fusion events, presumably resulting in gain of function, have also been reported. We present two pediatric soft-tissue sarcomas harboring a novel, recurrent in-frame fusion between SMARCA4 and VEZF1 (Vascular Endothelial Zinc Finger 1), a transcription factor important for vascular development and angiogenesis. The predicted fusion protein contains the N-terminal QLQ protein interaction domain of SMARCA4 and preserves most of VEZF1's C2H2 zinc-finger DNA-binding domains. Interestingly, another component of the BAF complex, SS18, has also been reported to be fused to VEZF1 in uterine sarcoma. We propose that fusion of BAF complex components to VEZF1 leads to aberrant recruitment of chromatin-remodeling activity to VEZF1 target loci, resulting in altered chromatin architecture, dysregulated VEZF1-dependent transcription, and tumorigenesis. - Source: PubMed
Fu LibingMao RongjunZhang ChangliangYang FanChen SiZhou DanXiao Sheng - Ferroptosis can be inhibited by insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3) in cancers. ETS variant transcription factor 4 (ETV4) is aberrantly expressed in various cancers. Elevated transcription of guanosine triphosphate cyclohydrolase 1 (GCH1) contributes to tumor malignancy. This study investigated the involvement of IGF2BP3, ETV4, and GCH1 in ferroptosis in gastric cancer (GC). - Source: PubMed
Publication date: 2026/05/01
Li KanWei HuiLi FangZheng YaZhou Yongning - Colorectal cancer (CRC) remains a leading cause of cancer-related mortality globally. Ferroptosis, a regulated form of cell death, has emerged as a promising frontier in CRC treatment. The transcriptional regulator ETV4 (ETS variant transcription factor 4) is implicated in CRC pathogenesis. However, its functional role has not been fully elucidated, and its potential to modulate ferroptosis in CRC is entirely unknown. This study aimed to investigate whether ETV4 modulates ferroptosis in CRC by regulating SLC7A11 and to explore the underlying mechanism involved. - Source: PubMed
Publication date: 2026/05/02
Chao ZhouzhouYin JinbaoHuang FengxiaXu JinlianLv YingyanChen JiayaoXu AijingZhu WeiWang Jinxing - Melanoma is an aggressive form of skin cancer with few effective treatments available at advanced stages. E26 transformation-specific translocation variant 4 (ETV4) is implicated in tumor progression in several malignancies. However, its role in melanoma and immune evasion remains poorly defined. The objective of this study was to investigate the expression and function of ETV4 in melanoma. ETV4 expression in melanoma tissues and cells was assessed by bioinformatics, quantitative PCR, Western blotting, and immunohistochemistry. Melanoma cell lines with ETV4 overexpression or knockdown were assessed for colony formation, wound healing, and Transwell migration/invasion. The regulatory relationship between ETV4 and integrin-associated protein (CD47) was investigated via dual-luciferase reporter assays and chromatin immunoprecipitation. Macrophage-mediated phagocytic activity was assessed using flow cytometry. ETV4 was markedly upregulated in melanoma tissues and cells, correlating with poor patient survival. Overexpression of ETV4 facilitates melanoma cell proliferation, migration, and invasion. Mechanistically, ETV4 directly bound to the CD47 promoter, transcriptionally activating its expression. ETV4 overexpression enhanced the phosphorylation of Src homology region 2 domain-containing phosphatase-1 and suppressed macrophage phagocytosis, suggesting activation of the CD47/signal regulatory protein α immune checkpoint pathway. Notably, knockdown of CD47 reversed the immunosuppressive effects induced by ETV4 overexpression, restoring macrophage phagocytic activity. ETV4 promotes melanoma progression and immune evasion by upregulating CD47 and activating the CD47/signal regulatory protein α signaling axis. Targeting the ETV4/CD47 pathway may represent a promising therapeutic option to enhance antitumor immunity in melanoma. - Source: PubMed
Publication date: 2026/04/27
Lu XuetaoChen MengFan HuayuGao ShuangshuangChen Jinguang