KCTD11 antibody - N-terminal region (ARP35623_T100)
- Known as:
- KCTD11 (anti-) - N-terminal region (ARP35623_T100)
- Catalog number:
- arp35623_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- KCTD11 antibody - N-terminal region (ARP35623_T100)
Related genes to: KCTD11 antibody - N-terminal region (ARP35623_T100)
- Gene:
- KCTD11 NIH gene
- Name:
- potassium channel tetramerization domain containing 11
- Previous symbol:
- C17orf36
- Synonyms:
- REN, KCASH1
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-10
- Date modifiied:
- 2016-10-05
Related products to: KCTD11 antibody - N-terminal region (ARP35623_T100)
Related articles to: KCTD11 antibody - N-terminal region (ARP35623_T100)
- N6-methyladenosine (m6A) plays a role in tumorigenesis of lung cancer (NSCLC); FTO functions as an oncogene in various cancers. However, the molecular mechanism underlying FTO-promoted lung cancer progression is still unclear. Gene expression was detected using RT-qPCR, western blot, and immunohistochemistry. The behaviors of lung cancer cells were detected using CCK-8, colony formation assay, and transwell assays. MeRIP and luciferase assays were conducted to FTO-mediated RNA hypomethylation. In vivo assays were performed to verify the roles of FTO in NSCLC. High levels of FTO in NSCLC patients predicted poor outcomes. However, FTO knockdown suppressed the proliferation and migration of A549 cells. Mechanically, FTO downregulated KCTD11 expression through promoting the RNA hypomethylation of KCTD11, the expression of which was decreased in NSCLC. KCTD11 knockdown attenuated the effects of FTO and promoted the malignancy of lung cancer. In summary, FTO functions as an oncogene in NSCLC via downregulating KCTD11. Therefore, FTO/KCTD11 can be a novel target for NSCLC. - Source: PubMed
Liu XinBai BingWei LiSong Zhengchang - Liver fibrosis is a pathological response following liver injury induced by various etiologies. Herein, we present the therapeutic potential of a novel anthraquinone compound, kanglexin (KLX), in the treatment of liver fibrosis. We observed significant suppression of the inflammatory response and extracellular matrix deposition in mice with liver fibrosis induced by CCL, by bile duct ligation, and by a methionine-choline-deficient diet. Mechanistically, through screening, we found that KLX interacts with HDAC1. Additionally, KLX facilitates binding between HDAC1 and KCTD11, promoting the ubiquitination-mediated degradation of HDAC1 and consequently reducing its protein level. Moreover, HDAC1 was found to bind to PPARγ, influencing its acetylation level. Following KLX treatment, the level of PPARγ deacetylation mediated by HDAC1 decreases, leading to increased protein expression of PPARγ. This effectively inhibited the NFκB and TGF-β/Smad2/3 signaling pathways, thereby reducing inflammation and extracellular matrix deposition. Ultimately, this intervention can halt the progression of liver fibrosis and ameliorate liver damage. In summary, our study demonstrated that KLX can effectively inhibit the progression of liver fibrosis by modulating the protein level and activity of HDAC1. These findings provide valuable insights for the development of effective drugs and treatment strategies for liver fibrosis. - Source: PubMed
Publication date: 2025/03/07
Zhang FengSong JinglunWu HanLin KeyingWang ChunleiZeng LinghuaKong XueZou KunkunDiao HongtaoWang ZhuoSi WeiJiang WeitaoYang YangYao FangtingZhang XinyueXiong YutingZhao QiaoyueDuo TianqiJu JiamingPan TengfeiYang BaofengBian Yu - The aim of the present work was to find an efficient method for safe and reliable expansion of human dental pulp cells (hDPCs) in vitro. Here, we examined the effect of a novel recombinant E8 fragment of Laminin-511 (iMatrix-511) in hDPCs regarding viability and cell spreading. Further, we investigated the underlying mechanisms governing its effects in hDPCs using RNA sequencing (RNA-seq). - Source: PubMed
Publication date: 2024/06/18
Tang JiaHuang Xiaofeng - Neurodegeneration is linked to the progressive loss of neural function and is associated with several diseases. Hypoxia is a hallmark in many of these diseases, and several therapies have been developed to treat this disease, including gene expression therapies that should be tightly controlled to avoid side effects. Cells experiencing hypoxia undergo a series of physiological responses that are induced by the activation of various transcription factors. Modulation of microRNA (miRNA) expression to alter transcriptional regulation has been demonstrated to be beneficial in treating multiple diseases, and in this study, we therefore explored potential miRNA candidates that could influence hypoxia-induced nerve cell death. Our data suggest that in mouse neuroblasts Neuro-2a cells with hypoxia/reoxygenation (H/R), miR-337-3p is downregulated to increase the expression of Potassium channel tetramerization domain containing 11 (KCTD11) and subsequently promote apoptosis. Here, we demonstrate for the first time that KCTD11 plays a role in the cellular response to hypoxia, and we also provide a possible regulatory mechanism by identifying the axis of miR-337-3p/KCTD11 as a promising candidate modulator of nerve cell survival after H/R exposure. - Source: PubMed
Zhu LinXin Yi-JuanHe MuBian JunCheng Xiao-LiLi RuiLi Jin-JieWang JuanLiu Jia-YunYang Liu - The Sonic Hedgehog (SHH) pathway is crucial regulator of embryonic development and stemness. Its alteration leads to medulloblastoma (MB), the most common malignant pediatric brain tumor. The SHH-MB subgroup is the best genetically characterized, however the molecular mechanisms responsible for its pathogenesis are not fully understood and therapeutic benefits are still limited. Here, we show that the pro-oncogenic stemness regulator Spalt-like transcriptional factor 4 (SALL4) is re-expressed in mouse SHH-MB models, and its high levels correlate with worse overall survival in SHH-MB patients. Proteomic analysis revealed that SALL4 interacts with REN/KCTD11 (here REN), a substrate receptor subunit of the Cullin3-RING ubiquitin ligase complex (CRL3) and a tumor suppressor lost in ~30% of human SHH-MBs. We demonstrate that CRL3 induces polyubiquitylation and degradation of wild type SALL4, but not of a SALL4 mutant lacking zinc finger cluster 1 domain (ΔZFC1). Interestingly, SALL4 binds GLI1 and cooperates with HDAC1 to potentiate GLI1 deacetylation and transcriptional activity. Notably, inhibition of SALL4 suppresses SHH-MB growth both in murine and patient-derived xenograft models. Our findings identify SALL4 as a CRL3 substrate and a promising therapeutic target in SHH-dependent cancers. - Source: PubMed
Publication date: 2023/12/07
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