TRAF6 antibody - middle region (ARP30226_P050)
- Known as:
- TRAF6 (anti-) - middle region (ARP30226_P050)
- Catalog number:
- arp30226_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TRAF6 antibody - middle region (ARP30226_P050)
Related genes to: TRAF6 antibody - middle region (ARP30226_P050)
- Gene:
- TRAF6 NIH gene
- Name:
- TNF receptor associated factor 6
- Previous symbol:
- -
- Synonyms:
- RNF85
- Chromosome:
- 11p12
- Locus Type:
- gene with protein product
- Date approved:
- 1997-06-12
- Date modifiied:
- 2015-11-20
Related products to: TRAF6 antibody - middle region (ARP30226_P050)
Related articles to: TRAF6 antibody - middle region (ARP30226_P050)
- Amplification of MYCN is a primary driver of aggressive retinoblastoma (RB), yet it remains a challenging therapeutic target. This study aimed to evaluate the therapeutic potential of the PROTAC molecule HLB-0532259 in degrading MYCN and suppressing RB growth. - Source: PubMed
Tang JunjieZhang ZhihuiLv JianjieWang MengSun HetianYao LanLi JinmiaoLiu YaomingHuang WeifengGao YangZhu YifanSu ShicaiLu Rong - Sepsis-associated encephalopathy (SAE) is a common and devastating manifestation of acute brain dysfunction in sepsis, yet mechanism-informed blood biomarkers with clinically interpretable diagnostic accuracy remain uncertain. A growing range of candidates spanning innate immune activation, blood-brain barrier dysfunction, glial response, and neuronal injury has been reported, but their comparative diagnostic performance and biological hierarchy are unclear, partly due to heterogeneity in phenotyping and sampling timing. - Source: PubMed
Publication date: 2026/08/03
Zhang QianZhu RunyingLi YiLi HuiLiu LixiaHu ZhenjieHuo Yan - An altered T-cell repertoire with aberrant immune activation is central to the pathogenesis of acquired aplastic anemia (aAA), and miRNAs are known to orchestrate T-cell activation; their relationship is, however, incompletely explored in aAA. The study aimed to validate specific miRNA-mRNA pairs involved in aberrant T-cell activation, differentiation, and cytokine levels in aAA. - Source: PubMed
Publication date: 2026/08/16
Sabereen GhazalaGupta RuchiSingh Manish KumarGupta KusumRahman KhaliqurChaturvedi Chandra PrakashChandra DineshKashyap Rajesh - Pediatric obstructive sleep apnea-hypopnea syndrome (OSAHS) associated with allergic rhinitis is characterized by persistent airway inflammation, in which the TLR4-MyD88-NF-κB signaling pathway plays a central role. Targeting this pathway may provide an effective strategy for modulating inflammatory responses. In the present study, an integrated computational and experimental approach was employed to identify and validate potential modulators of MyD88 signaling. De novo ligand design was performed to generate initial candidates, followed by artificial intelligence (AI)-based fragmentation and optimization to improve binding affinity and drug-like properties. Molecular docking and molecular dynamics simulations were conducted to evaluate binding stability and interaction profiles. The most promising compound was synthesized and structurally characterized using standard analytical techniques. Biological evaluation was performed across multiple in vitro models, including epithelial (RPMI 2650), macrophage (RAW 264.7), and mast cell (HMC-1) systems. Functional assays demonstrated that the optimized compound maintained cell viability while significantly reducing intracellular reactive oxygen species (ROS) levels. Western blot and quantitative PCR analyses revealed downregulation of key signaling components, including TLR4, MyD88, IRAK4, TRAF6, and NF-κB. In addition, ELISA-based cytokine profiling showed reduced levels of pro-inflammatory (TNF-α, IL-6, IL-1β) and Th2 cytokines (IL-4, IL-5, IL-13). Collectively, the findings indicate that the AI-fragmented lead compound was associated with attenuation of the TLR4-MyD88-NF-κB signaling axis across multiple biological levels. While further in vivo validation is required, this study highlights the potential of integrating AI-assisted drug design with experimental validation for the development of targeted therapeutics in inflammatory airway disorders. - Source: PubMed
Publication date: 2026/08/08
Gao JunSha XiaolanWang RongFu Yuanyuan - SASH1 (SAM [sterile alpha motif] and SH3 [SRC-homology-3] domain-containing protein 1) is a multidomain scaffold implicated in pigmentation, innate immunity, receptor signaling, cytoskeletal dynamics, vascular biology, and tumor suppression. Although genetic and expression studies link SASH1 dysfunction to diverse diseases, a unifying mechanistic framework has remained elusive. Here, we synthesize current knowledge of SASH1 structure, interaction networks, and biological functions across cell types and disease contexts. SASH1 contains an intrinsically disordered SPIDER (SLy Proteins Associated Disordered Region), an SH3 domain, two SAM domains, and multiple linear motifs; together, these elements mediate interactions with EphA8 (ephrin type-A receptor 8), β-arrestin 1, TRAF6 (TNF receptor-associated factor 6), CRKL (CRK-like proto-oncogene), IQGAP1 (IQ-motif-containing GTPase-activating protein 1), cortactin, and TNKS2 (tankyrase-2). We propose that SASH1 functions as a context-dependent multi-docking scaffold that organizes signaling architecture. Its modular domains, intrinsically disordered regions, and dual SAM domains enable flexible, multivalent interactions with partners that can be grouped into three functional modules: receptor regulation, intracellular signaling, and cytoskeletal organization. Notably, many SASH1 partners are themselves scaffold or adaptor proteins, allowing integration into pre-existing networks in a hierarchical 'scaffold-of-scaffolds' manner. Through selective partner recruitment, SASH1 links cell-surface receptor inputs to downstream signaling pathways and cytoskeletal remodeling. This model provides a mechanistic framework for how SASH1 drives diverse, cell-type-specific outputs across physiology and disease, while revealing broader principles by which multidomain scaffolds encode cellular behavior. - Source: PubMed
Publication date: 2026/08/06
Clements Christopher MRoney Md Saiful IslamShellman Yiqun G