ILF2 Antibody (AMM10107A)
- Known as:
- ILF2 Antibody (AMM10107A)
- Catalog number:
- amm10107a
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ILF2 Antibody (AMM10107A)
Related genes to: ILF2 Antibody (AMM10107A)
- Gene:
- ILF2 NIH gene
- Name:
- interleukin enhancer binding factor 2
- Previous symbol:
- -
- Synonyms:
- NF45
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-15
- Date modifiied:
- 2015-08-25
Related products to: ILF2 Antibody (AMM10107A)
Related articles to: ILF2 Antibody (AMM10107A)
- Intrahepatic cholangiocarcinoma (iCCA) represents an unmet clinical need due to its increasing incidence, aggressive biology, and limited treatment options. The extremely low-response rates to current systemic regimens and the emergence of adaptive resistance to targeted therapies underscore the urgent need for alternative therapeutic strategies. Given that the lineage-defining transcription factors SOX9 and YAP1 are central regulators of cholangiocyte and iCCA identity, we investigated their functional roles as potential therapeutic vulnerabilities across multiple preclinical models. - Source: PubMed
Publication date: 2026/04/03
Kim MinwookHu ShikaiPark YoojeongKwon JosephMolina LauraWang Li-JuLiu Jia-JunLiu SilviaSinghi AaturChiu Yu-ChiaoKo Sungjin - Protein phosphorylation regulates key events of male germ cell differentiation. In the testis, SRPK1 and PP1γ are involved in protamine phosphorylation and dephosphorylation, respectively, and their deregulation is linked to defective chromatin structure and male infertility. The aim of this study was to expand our knowledge on the molecular role of these phosphorylation-modulating proteins through the identification of novel partners in the testis, potentially supporting additional roles in sperm development. Using immunoprecipitation followed by LC-MS/MS, we identified yet undescribed interactions of SRPK1 and PP1γ with proteins involved in sperm formation and regulation of spermatogenic gene expression. We reported that SRPK1 interacts with the key splicing regulator ASF/SF2, as well as with other proteins involved in posttranscriptional regulation such as PABP1 or IGF2BP3. We showed that the testis-enriched isoform 2 of PP1γ (PP1γ2) interacts with PIHI1D1, part of the R2TP chaperone complex, and predicted that ZFR, NDUFB10 and ILF2 interactions with PP1γ2 happen within the C-terminal sequence which is specific of PP1γ2 proteoform. Both SRPK1 and PP1γ interactomes include ILF2 and TBLX1R1, with roles in gene expression regulation. Most of the identified proteins are known phosphoproteins in male germ cells, supporting a functional interaction. Overall, our results suggest additional roles for SRPK1 and PP1γ during spermatogenesis, shedding light into the orchestrated regulation of the complex mechanisms driving sperm formation. Data are available via ProteomeXchange with identifiers PXD054959 and PXD054960. SIGNIFICANCE OF THE STUDY: In the present work, we report the first testicular protein interactome of two broad phosphorylation-modulating proteins, the kinase SRPK1 and the phosphatase PP1γ, known to be essential regulators of chromatin remodeling during male germ cell development. Our novel protein-protein interactions reveal additional roles for SRPK1 and PP1γ in male germ cells, in key processes including splicing, gene expression, protein homeostasis, or formation of sperm-specific structures. Our data will therefore contribute to a better understanding of the complex and orchestrated molecular mechanisms controlling testicular activity and proper sperm formation. The lack of male germ cell-specific protein-protein interaction datasets currently challenges the research on the still largely unknown molecular mechanisms driving male germ cell differentiation. This jeopardizes exploratory approaches and in silico validations in a testis-specific manner, as most available datasets have been obtained in somatic cells. Thus, our protein-protein interaction data will be a useful resource to those interested in identifying the origins of male reproductive health problems related to protein phosphorylation. Furthermore, our analyses suggesting that some of these interactions may also occur in other organs extend the relevance of our findings to the broader scientific community. - Source: PubMed
Publication date: 2026/03/30
de la Iglesia AlbertoBlanco MélinaJodar MeritxellFeudjio OlivierLeduc MarjorieCastillo JuditCocquet JulieOliva Rafael - Alternative splicing patterns have diverged rapidly during vertebrate evolution. By integrating genome-wide predictions of stable RNA duplexes, alternative splicing profiles, and proximity ligation-detection of RNA-RNA interactions, we observe that the majority of long-range intronic RNA duplexes are mediated by inverted Alu-repeat elements, and that these structures are associated with divergent exon skipping patterns in primates. We further observe evidence that the RNA binding proteins HNRNPC, ILF2 and ILF3 directly control Alu duplex-associated alternative splicing levels. Collectively, our results provide evidence that Alu-derived RNA duplexes modulated by RNA binding proteins have contributed to the remarkable divergence in alternative splicing patterns during mammalian evolution. - Source: PubMed
Publication date: 2026/03/26
Lee HyunbeenCao XinangParada Guillermo ELi Jack DaiyangIosub Ira ABraunschweig UlrichRebelo KennyUle JernejWan YueBlencowe Benjamin J - Adenosine-to-inosine (A-to-I) RNA editing, catalyzed by adenosine deaminases acting on RNA (ADARs), is a widespread modification in metazoans. Cumulative evidence has revealed the altered A-to-I editing profiles in cancers, but the underlying mechanism remains unclear. Here, we discover the well-known histone lysine methyltransferase enhancer of zeste homologue 2 (EZH2) as an unexplored ADAR interactor and editing regulator in prostate cancer (PCa). Through competing with interleukin enhancer binding factor 2 (ILF2) for ADAR1 binding, EZH2 reshapes the substrate selectivity of ADAR1 and thus exhibits a bidirectional role in editing regulation. Moreover, EZH2 depletion induces the translational repression of transportin-1 (TRN1), which further results in the accumulation of cytoplasmic ADAR1p110 isoform to protect many oncogenic transcripts from degradation. Consistently, depletion of ADAR1 dramatically enhances the sensitivity of cancer cells and tumors to EZH2 selective degraders. Collectively, our study sheds new light on a link between two layers of epigenetic regulations at histone modification and RNA editing levels, demonstrates a previously uncharacterized role of EZH2 in RNA editing and mRNA stability independently of its lysine methyltransferase activity, and reveals the significance of EZH2-ADAR1 cascade in governing RNA editing and mRNA stability, which may provide additional perspectives for the advancement of EZH2-targeting cancer therapies. - Source: PubMed
Publication date: 2026/03/26
Yi YangLi YanqiangWang RuiYu XufenLiu QiYum ChaehyunZhang YangQiao YuanyuanSzczepanski AileenWu SiqiLi QiaqiaFazli LadanShen JiangchuanWang XinLi XiaolingMu PingSchaeffer Edward MHundley Heather ANiu HengyaoChinnaiyan Arul MWang LuShi JinjunJin JianDong XuesenZhao WeiChen KaifuCao Qi - Intrahepatic cholangiocarcinoma (iCCA) represents an unmet clinical need due to its increasing incidence, aggressive biology, and limited treatment options. The extremely low-response rates to current systemic regimens and the emergence of adaptive resistance to targeted therapies underscore the urgent need for alternative therapeutic strategies. Given that the lineage-defining transcription factors SOX9 and YAP1 are central regulators of cholangiocyte and iCCA identity, we investigated their functional roles as potential therapeutic vulnerabilities across multiple preclinical models. - Source: PubMed
Publication date: 2026/02/02
Kim MinwookHu ShikaiPark YoojeongKwon JosephMolina LauraWang Li-JuLiu Jia-JunLiu SilviaSinghi AaturChiu Yu-ChiaoKo Sungjin