TRIM25 / RNF147 antibody Host rabbit
- Known as:
- TRIM25 / RNF147 (anti-) Host host: rabbit
- Catalog number:
- 'ARP58105-P050
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- ACR
- Gene target:
- TRIM25 / RNF147 antibody Host rabbit
Related genes to: TRIM25 / RNF147 antibody Host rabbit
- Gene:
- TRIM25 NIH gene
- Name:
- tripartite motif containing 25
- Previous symbol:
- ZNF147
- Synonyms:
- EFP, RNF147
- Chromosome:
- 17q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-03-16
- Date modifiied:
- 2015-09-01
Related products to: TRIM25 / RNF147 antibody Host rabbit
Related articles to: TRIM25 / RNF147 antibody Host rabbit
- Ankylosing Spondylitis (AS) is a chronic inflammatory autoimmune rheumatic disease that primarily affects the spine and sacroiliac joints. This study aimed to investigate the expression levels of immune response-related genes, including , , , , , , and , as well as the serum levels of CXCL10 and SIRPA proteins in patients with AS. In addition, the potential diagnostic performance of these molecular and serum biomarkers in distinguishing patients with AS from healthy controls was evaluated. A total of 45 patients with AS and 44 healthy controls were included in the study. Immune-related gene expression levels were analyzed using RT-PCR. In addition, serum CXCL10 and SIRPA protein levels were evaluated using ELISA. The expression levels of , , , , and were significantly increased in patients with AS compared to healthy controls ( < 0.05). In contrast, no significant differences were detected in the expression levels of and . In the ROC analysis, the highest diagnostic performance was obtained for (AUC = 0.741), (AUC = 0.720), and (AUC = 0.722). Serum CXCL10 and SIRPA levels were not significantly different between the groups. In AS, genes particularly associated with NF-κB and interferon signaling pathways (, , , , and ) were found to be significantly altered, and these genes may serve as potential molecular biomarkers for AS. In contrast, the diagnostic power of serum protein biomarkers is limited. These findings indicate that the potential of these genes as biomarkers for AS pathogenesis should be further supported by advanced studies evaluating their expression levels. - Source: PubMed
Publication date: 2026/06/27
Dogan Sevil CeyhanAgbektas TugbaAtas MertKabak GoncaTas AycaSilig Yavuz - Small nucleolar RNAs (snoRNAs) play crucial regulatory roles in various cancers. However, the mechanisms by which snoRNAs regulate N6-methyladenosine (mA) modifications in colorectal cancer (CRC) remain unclear. This study systematically deciphered the precise interaction mechanism between and the mA reader IMP2 in CRC. We demonstrate that specifically stabilizes IMP2 to activate the PIK3CD-CHKA-Kennedy pathway in an mA-dependent manner, promoting endoplasmic reticulum stress (ERS) and phosphatidylcholine (PC) biosynthesis, thereby driving CRC. Conversely, the -targeting antisense oligonucleotide (ASO), ASO-78, effectively suppresses ERS and PC levels, inhibiting CRC progression. Mechanistically, , relying on the "UAAUGA" element in its C-D box region, specifically binds to the Lys221 ubiquitination site of IMP2, blocking TRIM25-mediated degradation of IMP2 and maintaining its stability. IMP2 enhanced the stability and translation of the target mRNAs and by recognizing their corresponding mA positions, mA-3208 and mA-1619, respectively, to reshape the phosphatidylcholine metabolite profile in CRC cells. In terms of potential therapeutic strategies, the ASO-78 can significantly inhibit CRC cell proliferation, reduce ERS levels, and decrease phosphatidylcholine content. The combination of ASO-78 and IMP2 inhibitor IMP2-IN1, by dual blocking of the -IMP2 axis, exhibits an excellent proliferation-inhibiting effect in CRC organoids. This study not only reveals a mechanism by which the -IMP2 interaction regulates CRC occurrence and development but also provides theoretical basis for innovative therapeutic strategies for precise targeting of tumor snoRNA-mA reader interactions. - Source: PubMed
Publication date: 2026/07/14
Zhao YingqiHu XiaoyunLi YalunZhang JingGuo HaoZhang YuyingWu TingGuo JinyuPeng YiChe YingZhu XianglongChen QiuchenGrieve DavidWei MinjieWu Huizhe - Myocardial microvascular injury plays a critical role in myocardial ischemia‑reperfusion injury (MI/RI), and ferroptosis has emerged as an important contributor to cardiac damage. Although Schizandrin A (Sch) possesses cardioprotective effects, its clinical application is limited by poor stability and low bioavailability. This study aimed to develop a CMEC‑targeted delivery system for Sch and evaluate its ability to attenuate ferroptosis in cardiac microvascular endothelial cells (CMECs), thereby alleviating MI/RI. - Source: PubMed
Publication date: 2026/07/09
Guan XueLi XiaoleiYang JingYang MiSun PengboLi KeMa YingqiuZeng KeZhao YingGao JingquanDuan WeiLi Hong - ISG15 represents a key ubiquitin-like modifier induced primarily by interferon signaling. ISG15 is synthesized as a precursor, processed to a mature form, and covalently conjugated to substrates through a dedicated E1-E2-E3 enzymatic cascade involving UBE1L, UBE2L6, and E3 ligases such as HERC5, TRIM25, and ARIH1. This modification is reversed by deISGylases, particularly the highly specific protease USP18, which also negatively regulates interferon signaling. ISGylation impacts diverse molecular and cellular processes, including protein stability and function, protein-protein interaction, autophagy, transcription/translation, DNA damage response, and innate immunity. Advances in chemical biology and mass spectrometry-based proteomics have enabled the characterization of enzymes involved in (de)ISGylation and mapping of ISGylated proteins and sites. Dysregulated ISGylation is implicated in cancer, infection, neurodegenerative disorders, and inflammatory diseases, underscoring its broad pathophysiological relevance. - Source: PubMed
Publication date: 2026/07/13
Shirley David JosephYoo Euna - Ribophagy is a crucial mechanism that maintains ribosome homeostasis in the cell by directing nonfunctional ribosomes to degradation via macroautophagy/autophagy. Impaired ribophagy may lead to ribosome quality control disorders and may consequently be associated with various diseases known as ribosomopathies. This topic has been actively studied over the past decade, but the complete mechanism of ribophagy is not fully understood. To study the mechanism of ribophagy, we performed a genome-wide CRISPR-Cas9-based screening using a fluorescent ribophagy reporter, which is a cell line with ribosomes carrying RPL29 fused with mCherry and GFP fluorescent proteins. Using the genome-wide Brunello library of guide RNAs, we identified the most promising targets for further study, including the ubiquitin ligase TRIM25, for which we have shown specific binding to the ribosome during ribophagy induction, leading to ubiquitination of the ribosome on the nascent peptide chain and degradation of the whole ribosome. Our findings also demonstrated that poly(I:C) treatment, which mimics viral infection, activates ribophagy in a TRIM25-dependent manner, suggesting the ribophagy pathway could be an antiviral defense mechanism. Taken together, we discovered a novel regulator of ribophagy, TRIM25, which provides new insights into the regulation of selective autophagy in the context of ribosomopathies. - Source: PubMed
Publication date: 2026/07/13
Golubeva JuliaMikhailov AlexeyShepelev NikitaPleshko ElizavetaGuseva EkaterinaSidorova VeraShagimardanova ElenaAndrianova NadezdaPlotnikov EgorKarpov DmitryNovikova SvetlanaZgoda VictorRubtsova MariaDontsova OlgaSergiev Petr