TRIM25 polyclonal antibody (A02)
- Known as:
- TRIM25 pab (anti-) (A02)
- Catalog number:
- H00007706-A02
- Product Quantity:
- 50 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- TRIM25 polyclonal antibody (A02)
Related genes to: TRIM25 polyclonal antibody (A02)
- Gene:
- ALG11 NIH gene
- Name:
- ALG11 alpha-1,2-mannosyltransferase
- Previous symbol:
- -
- Synonyms:
- KIAA0266, CDG1P
- Chromosome:
- 13q14.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-24
- Date modifiied:
- 2019-01-18
- Gene:
- ANKIB1 NIH gene
- Name:
- ankyrin repeat and IBR domain containing 1
- Previous symbol:
- -
- Synonyms:
- DKFZP434A0225, KIAA1386
- Chromosome:
- 7q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-02
- Date modifiied:
- 2016-10-05
- Gene:
- ANKS1A NIH gene
- Name:
- ankyrin repeat and sterile alpha motif domain containing 1A
- Previous symbol:
- ANKS1
- Synonyms:
- KIAA0229
- Chromosome:
- 6p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 2003-04-24
- Date modifiied:
- 2016-10-18
- Gene:
- APPBP2 NIH gene
- Name:
- amyloid beta precursor protein binding protein 2
- Previous symbol:
- -
- Synonyms:
- KIAA0228, Hs.84084, PAT1
- Chromosome:
- 17q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-25
- Date modifiied:
- 2016-01-21
- Gene:
- ARC NIH gene
- Name:
- activity regulated cytoskeleton associated protein
- Previous symbol:
- -
- Synonyms:
- KIAA0278, Arg3.1
- Chromosome:
- 8q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-23
- Date modifiied:
- 2016-06-24
Related products to: TRIM25 polyclonal antibody (A02)
Related articles to: TRIM25 polyclonal antibody (A02)
- The Nipah virus (NiV) matrix (M) protein, essential for viral assembly, has been increasingly recognized for its potential immunomodulatory functions. However, its role in modulating the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) signaling pathway-a central regulator of inflammation and innate immunity-remains poorly defined. Here, we demonstrate that NiV-M significantly promotes activation of the classical NF-κB pathway. Our data showed that NiV-M interacts with multiple cellular signaling molecules of the NF-κB pathway, including tripartite motif containing 25 (TRIM25), inhibitor of nuclear factor kappa-B kinase subunit alpha (IKKα), nuclear factor of kappa light polypeptide gene enhancer in B-cell inhibitor alpha (IκBα), and the p65 subunit of NF-κB. Further analyses revealed that NiV-M enhanced the E3 ubiquitin ligase activity of TRIM25, facilitating its interaction with both retinoic acid-inducible gene I (RIG-I) and TNF receptor-associated factor 2 (TRAF2), thereby promoting K63-linked ubiquitination of RIG-I and TRAF2. Moreover, NiV-M strengthened the interaction between IKKα and IKKβ, leading to enhanced IKK complex activity and accelerated degradation of IκBα. In addition, NiV-M promoted phosphorylation and nuclear translocation of p65, thereby amplifying NF-κB-driven gene expression. In summary, our results demonstrate a multifaceted strategy by which NiV-M regulates the NF-κB pathway, a mechanism that may contribute to NiV pathogenesis via inflammatory dysregulation. These findings suggest potential therapeutic approaches for alleviating symptoms associated with immunopathology of NiV by targeting virus-host interactions.IMPORTANCEThis study reveals a previously unknown role of the Nipah virus matrix (M) protein in driving excessive inflammation, a key factor in the virus's high mortality. We discovered that the M protein acts as a master switch, hijacking a central human immune pathway (NF-κB) at multiple points to trigger a "cytokine storm." This explains how the virus causes severe tissue damage and organ failure in infected individuals. By identifying the specific human proteins targeted by the M protein, our work establishes that this viral component functions not only in viral assembly but also in the dysregulation of host inflammatory responses, thereby providing a new perspective on its potential contribution to severe NiV-associated disease. These findings open new avenues for treating NiV infections by developing drugs that target these interactions, potentially controlling the devastating inflammation rather than just the virus itself. - Source: PubMed
Publication date: 2026/05/21
Ye ChangMa XiaoyuKe XianliangYao ZhongziLiu RenyiLi TianZhang PeiluWakjira Bayeta SenbetaTang ShixiangLiu FengYe ZiXie YingChen Quanjiao - Hepatitis B virus (HBV) is the primary driver of liver cancer (LC), a malignancy characterized by extensive metabolic reprogramming. However, the specific mechanisms linking viral oncoproteins to metabolic dysregulation in LC remain incompletely understood. This study was aimed at investigating the function of the metabolic enzyme GPT2 in hepatocarcinogenesis, focusing on its regulation by HBV X protein (HBx) and its effects on downstream signaling pathways. - Source: PubMed
Publication date: 2026/05/19
You HongjuanWang XingLiu RuyuWang YuxinZhang HuanyangMa LihongBao EnsiZhong YujieLiu XiangyeKong DelongPan XiuchengLi XiaocuiQin SupingZheng KuiyangLi ChenTang RenxianKong Fanyun - Fibrosis represents a complex pathological process that culminates in organ damage and failure. Cataract, specifically anterior subcapsular cataract (ASC) and posterior capsular opacity (PCO), is a common manifestation of ocular fibrosis, primarily driven by the epithelial mesenchymal transition (EMT) of lens epithelial cells (LECs). Tripartite motif containing 25 (TRIM25), an E3 ubiquitin ligase and member of the TRIM protein family, plays a pivotal role in various biological processes including protein homeostasis, signaling pathways, immune responses, and cell growth. This study aims to elucidate the role of TRIM25 in LECs EMT and its underlying molecular mechanisms, thereby identifying a novel therapeutic target for the prevention and treatment of fibrotic cataracts. - Source: PubMed
Publication date: 2026/05/15
Liu YifanHuang YihanChen AnlinHan LeiBian LiXu XuanLi Yue - Ferroptosis, a unique form of regulated cell death induced by iron-dependent lipid peroxidation, has been implicated in the pathogenesis of Mycobacterium tuberculosis (Mtb). However, the role of Mtb proteins, particularly those encoded by the genomic regions of deletion (RDs), involved in mediating macrophage ferroptosis has not been thoroughly investigated. This study aimed to screen for Mtb RD region-encoded proteins that induce macrophage ferroptosis and elucidate the underlying molecular mechanisms. - Source: PubMed
Publication date: 2026/05/11
Qu ZiluZhou YuanyuanCai QinzhenChen TianXiang YunChen LiuqingYuan Chunhui - Diabetes-associated cognitive dysfunction (DACD) is a severe neurological complication of type 2 diabetes. Impaired autophagic flux is a critical contributor to the progression of DACD. This study aimed to clarify how tripartite motif-containing 25 (TRIM25) regulates autophagy in DACD. To mimic the hyperglycemic environment of diabetes, HT22 hippocampal neurons were exposed to high glucose (HG). Autophagic flux was monitored using an RFP-GFP-LC3 reporter. Transcriptional regulation was evaluated using chromatin immunoprecipitation and a dual-luciferase reporter assay. Protein stability and ubiquitination were examined using a cycloheximide chase assay and co-immunoprecipitation. Protein abundance was determined by western blot, whereas mRNA levels were quantified by reverse transcription quantitative polymerase chain reaction. In HT22 hippocampal neurons exposed to HG, TRIM25 expression was significantly upregulated, whereas sine oculis homeobox 2 (SIX2) and sprouty-related EVH1 domain-containing protein 2 (SPRED2) expression was significantly downregulated. TRIM25 directly interacted with SIX2 and promoted its ubiquitination and degradation. Moreover, TRIM25 inhibited neuronal autophagy under HG conditions by targeting SIX2. SIX2 transcriptionally activated SPRED2 expression and subsequently inhibited extracellular signal-regulated kinase (ERK) phosphorylation. HG-induced reductions in cell viability and autophagy were reversed by SIX2 overexpression but not when SPRED2 was simultaneously knocked down. TRIM25 reduces SPRED2 transcription by mediating the ubiquitination and degradation of SIX2, thereby exacerbating the suppression of neuronal autophagy under high-glucose conditions. This study identifies a novel TRIM25/SIX2/SPRED2/ERK axis through which hyperglycemia impairs neuronal autophagy. - Source: PubMed
Publication date: 2026/05/09
Chen LiZhou XiankeTan HongBao