Active PKC iota
- Known as:
- Active PKC iota
- Catalog number:
- ASAPPK-466Z
- Product Quantity:
- 5 µg
- Category:
- -
- Supplier:
- Other suppliers
- Gene target:
- Active PKC iota
Related genes to: Active PKC iota
- Gene:
- NLRP14 NIH gene
- Name:
- NLR family pyrin domain containing 14
- Previous symbol:
- NALP14
- Synonyms:
- NOD5, GC-LRR, Nalp-iota, PAN8, CLR11.2
- Chromosome:
- 11p15.4
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-28
- Date modifiied:
- 2016-06-01
Related products to: Active PKC iota
10” active carbon block filter10” granular active carbon filter10”granular active carbon filter17 kDa PKC-potentiated inhibitory protein of PP1,Cpi,Cpi17,CPI-17,Ppp1r14a,Protein kinase C-potentiated inhibitor protein of 17 kDa,Protein phosphatase 1 regulatory subunit 14A,Rat,Rattus norvegicus17 kDa PKC-potentiated inhibitory protein of PP1,CPI17,CPI-17,Homo sapiens,Human,PPP1INL,PPP1R14A,Protein kinase C-potentiated inhibitor protein of 17 kDa,Protein phosphatase 1 regulatory subunit 14A17 kDa PKC-potentiated inhibitory protein of PP1,Cpi17,CPI-17,Mouse,Mus musculus,Ppp1r14a,Protein kinase C-potentiated inhibitor protein of 17 kDa,Protein phosphatase 1 regulatory subunit 14A17 kDa PKC-potentiated inhibitory protein of PP1,CPI17,CPI-17,Pig,Protein kinase C-potentiated inhibitor protein of 17 kDa,Protein phosphatase 1 regulatory subunit 14A,Sus scrofa27 kDa prosomal protein,Homo sapiens,Human,Macropain iota chain,Multicatalytic endopeptidase complex iota chain,p27K,PROS27,PROS-27,Proteasome iota chain,Proteasome subunit alpha type-6,PSMA62_Chloro_4,6_bis(ethylamino)_sym_triazine 80% active2_Chloro_4,6_bis(ethylamino)_sym_triazine 80% active2_Chloro_4,6_bis(ethylamino)_sym_triazine 80% active3_Phosphoinositide Dependent Protein Kinase_1 (PDK1&_65292;active)A murine NKX2-8 was isolated from the Hepal-6 cell line and showed oligonucleotide binding competitive with fetoprotein transcription factor. Nkx2.8 bound to the active AFP promoter, and antisense inhA20 (E. coli) Active Human Recombinant ProteinA20 (E. coli), Active Human Recombinant Protein Related articles to: Active PKC iota
- As an important member of non-coding RNAs, lncRNAs play a significant role in various biological processes, including regulating the immune response after bacterial infection. In this study, we identified a novel lncRNA () in turbot (). As a result, was more than 2234 bp in length and was detectable in the liver, spleen, head kidney, intestine, skin, gill, muscles, blood, and brain, with the highest expression levels in the blood, followed by the spleen. To better understand the biological significance of lncRNAs in the immune system, this study performed qPCR on mucosal tissues (intestine, skin, and gill) at 0, 2, 6, 12, 24, and 48 h after () infection. Following infection with , the expression of was significantly upregulated in the skin but significantly downregulated in the gill. Given that lncRNAs can regulate target genes through different mechanisms depending on their subcellular localization, we explored the localization of . Both RNA nucleoplasmic isolation and experiments showed that was predominantly localized in the nucleus. GO and KEGG analyses indicated that was involved in several pathways related to the immune response such as the Tight junction, the Ras signaling pathway, and the Rap1 signaling pathway. Moreover, overexpression of in SMK cells significantly upregulated all tested immune genes, and this effect was further enhanced upon LPS stimulation at 6 h, suggesting a potential regulatory role for in the immune system. Meanwhile, it was found that overexpression of could activate the promoter activity of gene and inhibit the NF-κB activity. The above results enrich the information of lncRNAs in teleost and provide a resource base for further research on the immune function of lncRNAs. - Source: PubMed
Publication date: 2026/05/08
Wang BeibeiLiu YiyingLi YangLiu XiaoliYang NingLi Chao - Zygotic genome activation (ZGA) is essential for initiating the developmental gene expression program in early embryos. However, whether a gating mechanism orchestrated by a limited number of factors exists in mammals remains debated. In this study, by utilizing an Nlrp14-deficient model that intriguingly disrupts the zygotic localization of UHRF1 and DNMT1, and in combination with comprehensive genetic approaches, we demonstrated that the nuclear exclusion of UHRF1 is essential for mouse ZGA and subsequent developmental progression. Mechanistically, the failure to exclude UHRF1 and DNMT1 from the nucleus in zygotes would impede DNA demethylation in LINE1 elements, promote UHRF1 binding to silence their expression, thereby reducing global chromatin accessibility and inhibiting ZGA. This effect was rescued in Uhrf1/Nlrp14 double knockout (DKO) embryos, which still exhibited heavy DNA methylation, highlighting a dispensable role of UHRF1 in the maintenance of genome-wide DNA methylation after fertilization. Furthermore, reducing DNA methylation through Dnmt1/Nlrp14 DKO or inhibiting the DNA methylation-binding domains of UHRF1 mitigated the adverse effects of nuclear-localized UHRF1 and reactivated the ZGA genes. Finally, we demonstrated that the residual nuclear UHRF1 in normal embryos binds to and facilitates the transcriptional inactivation of specific LTR subtypes that evade DNA demethylation during the genome-wide epigenetic reprogramming. Our findings not only highlight the biological significance of UHRF1 and DNMT1 nuclear exclusion but also elucidate the potentially conserved mechanism that regulates ZGA during mammalian preimplantation development. - Source: PubMed
Publication date: 2026/05/26
Yan RuiCheng XinLong XinZhu YatingZhang QianchengSun FengyuanZhang FanWang MengyueZhang RuifengGuo TianziHou XinlingJi DongmeiCao YunxiaGao FeiLiang DanGuo Fan - NLRP14 is an essential maternal factor for mammalian embryonic development. Maternal ablation of NLRP14 in mice impairs DNA demethylation and calcium homeostasis in zygotes, causing early embryonic arrest. However, the underlying biochemical events remain largely unknown. Here, we identified two binding partners (KDM2A and UHRF1) of NLRP14 and further solved structures of NLRP14-KDM2A-SKP1 and NLRP14-UHRF1. Structural analysis revealed that NLRP14 modulates the SKP1-CUL1-F-box (SCF) E3 ubiquitin ligase and the RING-type E3 ubiquitin ligase UHRF1 through two distinct mechanisms. Mechanistically, NLRP14 competitively inhibits KDM2A-mediated SCF assembly or allosterically inhibits the activity of UHRF1 by occupying the E2 ubiquitin-conjugating enzyme (UBE2D) binding site of the ubiquitin-like (UBL) domain. Deletion of NLRP14 in mice increases ubiquitination levels in oocytes during maturation and after fertilization. Collectively, our findings identify NLRP14 as a dual regulator that restrains E3 ubiquitin ligase-driven ubiquitination by limiting SCF complex assembly and attenuating UHRF1 activity. This regulatory role is required to prevent excessive protein ubiquitination and maintain proteostasis during the oocyte-to-embryo transition, thereby supporting early embryonic development. Our study uncovers maternal regulation of proteostasis in oocytes and suggests that dysregulating proteostasis is an important factor in the pathogenesis of reproductive disorders. - Source: PubMed
Publication date: 2026/04/08
Liu SibeiQi QianqianChi PengliangJiao HaizhanYan LiLu YuechaoZhang RongrongLi JinhongJu SichengHan ZhuoZhang ZihanLiu QingtingOu GuojinLi JialuChen JingWang XiangLi LeiGuo LiJiao XueHu HongliJiang YongmeiDeng Dong - Sex chromosomes in amphibians exhibit substantial variability and often remain largely homomorphic, providing a powerful system for studying sex determination. The Sangzhi horned toad (Boulenophrys sangzhiensis) is an ideal model, but limited genomic resources have hindered insights into sex determination mechanisms. Here, we assembled a 2.8 Gb chromosome-level genome of B. sangzhiensis generated using PacBio HiFi and Hi-C data, achieving a Contig N50 of 30 Mb and identifying 21,775 protein-coding genes. Genome-wide analyses of coverage, F, SNP density, and linkage disequilibrium identified two putative sex-linked regions on chromosome 2 and 6, showing sex-specific coverage and strong genetic differentiation. Within these sex-linked regions, we identified a Y-specific sequence and several candidate sex-determining genes, including Hsd11b2, Nlrp14, and zinc finger genes. Our findings suggest that sex determination in B. sangzhiensis involves a complex, possibly polymorphic mechanism, with multiple Y haplotypes segregating within populations. Additionally, the sex-linked regions exhibit accumulation of repetitive sequences, multi-copy genes, and chromosomal rearrangements, which may contribute to the evolution of sex chromosomes. This chromosome-level genome provides a valuable resource for understanding the dynamic evolution of sex-determining mechanisms in amphibians. - Source: PubMed
Huang Chun HXie Si YLi JunChen Wan YQiu Fu YZhao MianLiu WeiLiao Chun LWu Hua - The fertilized egg relies almost entirely on maternal stores in the oocyte to ensure the successful initiation of development. The cytoplasmic lattices (CPLs) in mammalian oocytes store maternal-expressed proteins and have an essential role in embryogenesis. Impairing multiple CPL members leads to early embryonic arrest, resulting in infertility in mammals. However, the mechanism underlying the assembly and storage of CPLs remains largely unknown. Here we report the cryo-electron microscopy structure of a native mouse CPL repeating unit (approximately 4 MDa) at 3.74 Å resolution. This repeating unit exhibits a tripartite architecture comprising a framework, extended linkers and a CPL core. The external framework is built from PADI6 decamers and the subcortical maternal complexes. Two linkers formed by NLRP4F polymerize the frameworks into an extended filament. In the CPL core, the epigenetic regulator UHRF1 is trapped by PADI6, UBE2D and NLRP14 in a compact, autoinhibited conformation that prevents nuclear entry and ubiquitin ligase activity. Moreover, the CPL core stores GTP-bound α/β-tubulin heterodimers and inactive SCF E3-ubiquitin ligase components (FBXW-SKP1 complex) in a poised but restrained state. These features establish CPLs as a dynamic regulatory pool that enables rapid microtubule assembly and tightly controlled ubiquitination during the oocyte-to-embryo transition. Together, this semi-in situ structure illuminates CPL assembly and storage-module organization, and establishes CPLs as specialized proteostasis organelles for maternal regulation in oocytes and early embryonic development. - Source: PubMed
Publication date: 2026/03/31
Chi PengliangWang XiangLi JialuHuang JingruiJu SichengLiu SibeiYan LiLu YuechaoZhang ZihanHan ZhuoLi JinhongQi QianqianLiu QingtingZeng YirenGuo LiZhang XiaofengGui LongDeng Dong