RNF126 Antibody (monoclonal) (M03)
- Known as:
- RNF126 Antibody (mab) (M03)
- Catalog number:
- AT3662a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- RNF126 Antibody (monoclonal) (M03)
Related genes to: RNF126 Antibody (monoclonal) (M03)
- Gene:
- CENPJ NIH gene
- Name:
- centromere protein J
- Previous symbol:
- MCPH6
- Synonyms:
- CPAP, BM032, LAP, LIP1, Sas-4, SASS4, SCKL4
- Chromosome:
- 13q12.12-q12.13
- Locus Type:
- gene with protein product
- Date approved:
- 2002-02-15
- Date modifiied:
- 2018-02-13
- Gene:
- CENPN NIH gene
- Name:
- centromere protein N
- Previous symbol:
- C16orf60
- Synonyms:
- FLJ13607, FLJ22660, BM039
- Chromosome:
- 16q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-20
- Date modifiied:
- 2015-08-24
- Gene:
- DONSON NIH gene
- Name:
- downstream neighbor of SON
- Previous symbol:
- C21orf60
- Synonyms:
- B17, C2TA, DKFZP434M035
- Chromosome:
- 21q22.11
- Locus Type:
- gene with protein product
- Date approved:
- 2000-02-18
- Date modifiied:
- 2017-03-30
- Gene:
- EAPP NIH gene
- Name:
- E2F associated phosphoprotein
- Previous symbol:
- C14orf11
- Synonyms:
- BM036, FLJ20578
- Chromosome:
- 14q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-11-18
- Date modifiied:
- 2016-02-26
- Gene:
- GOLGA2P5 NIH gene
- Name:
- GOLGA2 pseudogene 5
- Previous symbol:
- GOLGA2L1, GOLGA2B
- Synonyms:
- DKFZp434M0331
- Chromosome:
- 12q23.1
- Locus Type:
- pseudogene
- Date approved:
- 2006-01-27
- Date modifiied:
- 2018-04-26
Related products to: RNF126 Antibody (monoclonal) (M03)
Related articles to: RNF126 Antibody (monoclonal) (M03)
- Ring finger protein 126 (RNF126) is a RING-type E3 ubiquitin ligase that has recently emerged as a multifaceted regulator of cellular homeostasis, stress adaptation, and disease progression. Through its structurally distinct zinc-finger and catalytic RING domains, RNF126 orchestrates substrate recognition and ubiquitin transfer, generating diverse ubiquitin linkages with both proteolytic and nonproteolytic functions. Initially characterized as a component of the protein quality control (PQC) machinery, RNF126 cooperates with chaperones such as BAG6 and UBQLN1 to eliminate mislocalized and misfolded proteins, thereby maintaining proteostasis. Beyond PQC, RNF126 plays pivotal roles in DNA damage response pathways by regulating homologous recombination, non-homologous end joining, checkpoint signaling, and genome stability through substrates, including MRE11, Ku80, RNF168, and 14-3-3σ. Genetic studies have further demonstrated its importance in embryogenesis and male fertility, and accumulating evidence has identified RNF126 as a critical driver of malignancy in multiple cancers. RNF126 promotes tumor progression by degrading or modulating key regulators, such as p21, PTEN, p53, PDKs, and LKB1, thereby enhancing proliferation, metabolic reprogramming, anoikis resistance, metastasis, and chemo/radioresistance. Intriguingly, RNF126 exhibits context-dependent functions, acting as an oncogene or tumor suppressor depending on the tissue type and substrate selection. In addition to cancer, RNF126 has been implicated in neurodegeneration, cardiac pathology, antiviral immunity and adaptive immune regulation. This review summarizes the current knowledge of RNF126 structure, ubiquitin signaling mechanisms, physiological functions, and pathological roles, while discussing emerging therapeutic strategies and future challenges for targeting RNF126 in precision medicine. - Source: PubMed
Publication date: 2026/06/25
Vu Anh DucMori ShioriSakamoto Takeharu - The mechanistic target of rapamycin complex 1 (mTORC1) serves as a central metabolic hub that integrates nutrient signals and orchestrates cellular metabolism to regulate many fundamental cell processes. While mTORC1 activation is known to occur both on lysosomal membranes and at the Golgi apparatus in response to environmental cues, the molecular mechanisms governing its Golgi-associated activation remain poorly understood. In this study, we identified YIF1A as a novel Golgi-localized regulator of growth factor-mediated mTORC1 signaling. Mechanistically, YIF1A interacted with the E3 ubiquitin ligase RNF126 to facilitate K48-linked polyubiquitination of G3BP1/2, thereby promoting mTORC1 activation. Genetic depletion of either YIF1A or RNF126 stabilized G3BP1/2 proteins and significantly impaired mTORC1 activity. Notably, YIF1A knockdown conferred resistance to etoposide- and doxorubicin-induced cellular senescence. The evolutionary conservation of this pathway was demonstrated by extended or shortened lifespan in Caenorhabditis elegans lacking or overexpressing yif-1, the invertebrate ortholog of YIF1A. Our findings not only elucidate a previously unrecognized Golgi-specific regulatory axis for mTORC1 activation but also suggest YIF1A as a potential therapeutic target for modulating aging-related pathologies. - Source: PubMed
Publication date: 2026/06/23
Zhang XiaogangLiu LuyingShang MengdiHu BinZhu ShuWang XiLiu JieyingHan YanchunWei XiaodanCao QiLi FanGao LijieSun JingyuYu JiaqiTan ChentaiDong MenghuaTang Tie-ShanWang Jiu-Qiang - Fetal growth restriction (FGR) remains a major contributor to neonatal morbidity and mortality worldwide, with limited effective diagnostic and therapeutic options. To better understand its molecular mechanism, we performed integrated multi-omics analyses of placental tissues from FGR pregnancies and normal controls, identifying Ring Finger Protein 126 (RNF126), an E3 ubiquitin ligase, as a key regulator of FGR and a potential biomarker distinguishing FGR from small-for-gestational-age (SGA) fetuses. Placenta-specific RNF126 conditional knockout (cKO) mice demonstrated a causal role of elevated placental RNF126 in FGR development . Functional studies revealed that RNF126 induced endoplasmic reticulum (ER) stress and apoptosis in trophoblasts. Mechanistically, RNF126 promoted a ubiquitin-proteasome-mediated degradation of the MYH9/MYH10 complex, thereby exacerbating ER stress and impairing trophoblast function, with lysine 833 (K833) of MYH9 identified as a critical ubiquitination site. Collectively, these findings elucidate an RNF126-mediated pathogenic mechanism in FGR and highlight RNF126 as a promising biomarker and therapeutic target. - Source: PubMed
Publication date: 2026/06/08
Lu LilinYe XiaomeiLan JiawenXu ShuxiuCheng ManyuLv ChenlinZhou JunLi Jing - Myeloid differentiation factor 88 (MyD88) is a critical mediator of inflammatory signaling. However, the development of MyD88 inhibitors has been limited, and there are no reports on MyD88 degraders. Based on our previously identified MyD88 inhibitor and employing a template-assisted modification strategy, we designed and synthesized 40 novel derivatives, and identified the optimal compound , which could inhibit nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) pathway activation by facilitating the interaction between ring finger protein 126 (RNF126) (an E3 ubiquitin ligase) and MyD88, thereby promoting ubiquitination and subsequent degradation of MyD88. The subacute toxicity test indicated that had good safety profile. Furthermore, it demonstrated significant anti-inflammatory effects in both cecal ligation and puncture (CLP) and lipopolysaccharide (LPS) induced acute lung injury (ALI) models, effectively ameliorating ALI symptoms. These findings suggest that holds considerable promise as a MyD88-targeting molecular glue degrader for the treatment of ALI. - Source: PubMed
Publication date: 2026/06/12
Zhu LuxiaoTang DanChen TingSun ChenhuiDong KeChen QiDai QinxueMo YunchangChen PanSun JinfengLiang GuangTang Qidong - Tumor hypoxia promotes dedifferentiation and metabolic reprogramming in hepatocellular carcinoma (HCC), undermining normal liver functions. Here, we identify the E3 ubiquitin ligase RNF126 as a hypoxia-inducible "peroxisomal fate" switch that links the hypoxic microenvironment to loss of hepatocyte differentiation. Under hypoxia, HIF-2α drives RNF126 expression, which in turn ubiquitinates the peroxisomal membrane transporter ABCD3, triggering selective peroxisome autophagy (pexophagy) and depletion of peroxisomes. This organelle loss ablates very-long-chain fatty acid β-oxidation and hydrogen peroxide detoxification, erasing key hepatocyte differentiation features. We show that genetic RNF126 ablation restores peroxisomal functions and impairs hypoxic HCC growth. Leveraging these insights, we developed a small-molecule RNF126 inhibitor, D665-1412, which selectively blocks hypoxia-induced pexophagy. D665-1412 treatment stabilizes peroxisomes, normalizes lipid metabolism, and reactivates hepatocytic differentiation markers, thereby "redifferentiating" HCC cells and suppressing tumor progression in vitro and in vivo. Our findings establish the HIF-2α-RNF126-ABCD3 axis as a driver of HCC dedifferentiation and present organelle-targeted redifferentiation therapy as a promising approach for liver cancer. - Source: PubMed
Publication date: 2026/06/09
Su QiYang YichunRen JiayanZhang YuFu LijuanWu QingHan XuZhang Yanmin