BMI1 Antibody
- Known as:
- BMI1 Antibody
- Catalog number:
- 32015
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- BMI1 Antibody
Related genes to: BMI1 Antibody
- Gene:
- BMI1 NIH gene
- Name:
- BMI1 proto-oncogene, polycomb ring finger
- Previous symbol:
- PCGF4
- Synonyms:
- RNF51
- Chromosome:
- 10p12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-05
- Date modifiied:
- 2016-10-05
Related products to: BMI1 Antibody
Related articles to: BMI1 Antibody
- Increasing evidence indicates that long non-coding RNAs (lncRNAs) play a regulatory role in plant responses to environmental stress. However, the epigenetic mechanisms behind the regulation of salt stress by lncRNAs remain largely elusive. We previously discovered that the lncRNA MtCIR2 of Medicago trnucatula negatively regulated seed germination under salt stress by altering endogenous ABA and GA concentrations via histone ubiquitination. Here we evaluated the roles of MtCIR2 in regulating response of M. truncatula seedlings to salt stress. We found that over-expression and mutation of MtCIR2 reduced and enhanced tolerance to salt stress due to enhanced and suppressed foliar Na accumulation in over-expression and Mtcir2 mutant plants relative to their wild-type counterparts under salt stress. The MtCIR2-depenent Na accumulation was accounted for by the suppression of MtSOS2 that encodes a kinase responsible for Na exclusion from plants. We discovered that MtCIR2 physically interacted with BMI1, a core component of Polycomb Repressive Complex 1 (PRC1), leading to down-regulation of MtSOS2. ChIP assays revealed that MtCIR2 facilitated H2A ubiquitination at the chromatin of MtSOS2, thus repressing its expression, which in turn suppressed the SOS-dependent Na exclusion, and rendered the plants sensitive to salt stress. These results unravel a novel mechanism by which lncRNA epigenetically regulates SOS-mediated Na accumulation via histone ubiquitination in plant response to salt stress. - Source: PubMed
Publication date: 2026/09/23
Sun XiaohanTian RuiZhao MinguiZhang Wen-Hao - Despite the contribution of cancer stem-like cells (CSLCs) to acquired paclitaxel resistance in non-small cell lung cancer (NSCLC), the biomarkers and regulatory mechanisms sustaining their stemness under chemotherapy pressure remain poorly understood. This study aimed to identify the stemness-maintaining programs underlying CSLC-associated paclitaxel resistance. Paclitaxel-resistant NSCLC cell models were established. RNA-seq data from resistant spheres and adherent resistant cells were integrated with Gene Ontology/Kyoto Encyclopedia of Genes and Genomes/gene set enrichment analysis and patient transcriptomic datasets to identify CSLC maintenance-associated candidate biomarkers. Inhibitors, sphere-forming assays, CD104CD166CD49f flow cytometry, reverse transcription quantitative polymerase chain reaction, western blotting, and ST6GAL1 knockdown or overexpression were used for functional and mechanistic validation. Sambucus nigra agglutinin lectin blotting was performed to assess epidermal growth factor receptor (EGFR) α2,6-sialylation. Clinical relevance was assessed using ST6GAL1 immunohistochemistry on 46 clinical lung tumor tissues. Paclitaxel-resistant NSCLC cells exhibited enhanced sphere formation and CD104CD166CD49f expansion. N-glycosylation was activated in resistant spheres. A seven-gene N-glycosylation signature was identified as a CSLC-associated candidate biomarker in acquired paclitaxel resistance. Inhibiting N-glycosylation suppressed the EGFR-mTOR-SOX2/BMI1 axis, decreased CSLCs, and restored paclitaxel sensitivity. ST6GAL1 regulated EGFR α2,6-sialylation. ST6GAL1 depletion also decreased EGFR abundance, suppressed mTOR-SOX2/BMI1 signaling, and sensitized paclitaxel-resistant spheres to paclitaxel rather than adherent cells. ST6GAL1 expression, which was higher in tumors from patients who underwent chemotherapy, showed a trend toward poorer survival among chemotherapy-treated patients. The seven-gene signature was associated with shorter disease-free survival but not overall survival in lung cancer patients. ST6GAL1-mediated α2,6-sialylation of EGFR contributes to the maintenance of CSLC-associated paclitaxel resistance through mTOR-SOX2/BMI1 signaling. These findings identify ST6GAL1-dependent EGFR sialylation as a potential therapeutic target in CSLC-associated chemoresistance. - Source: PubMed
Publication date: 2026/08/31
Yang YuxiLiang BinghuiHong WeijieLee Sau HarTang DongfangXie ShuxianQin ChangtaiShen LiuSun ZhumeiYan XiaofengLi HuaWang XiaolingHu XudongYe TingjieZhang WeiXu Wei - Canonical Polycomb repressive complex 1 (cPRC1) preserves cell fate decisions by repressing aberrant transcription of developmental regulator genes. We report the cryo-electron microscopy structure of the human cPRC1 holocomplex assembled from RING1B, BMI1, PHC2 and CBX7 bound to an H3K27me3-modified mononucleosome together with the ubiquitin-conjugating enzyme UBCH5C. cPRC1 adopts a compact, highly integrated architecture in which the subunits RING1B, BMI1 and PHC2 form an extended interface that positions UBCH5C on the nucleosome to enable efficient monoubiquitination of histone H2A at K119. This organization is conserved in Drosophila, where mutational analyses identify the PHC2 ortholog Polyhomeotic (Ph) as a central scaffold and targeting factor. The Ph HD domain is required for complex assembly, whereas the Ph SAM domain is dispensable for assembly but essential for cPRC1 recruitment to Polycomb target genes and productive H2A monoubiquitination at these loci. - Source: PubMed
Publication date: 2026/09/14
Ciapponi MariaCafiso MartinaSchkölziger SvenBenda ChristianBonnet JacquesMüller Jürg - The abrupt transition in feed composition and form during the starter (d 0 to 10) to grower (d 11 to 21) phase can damage intestinal barriers and affect broiler performance, triggering the feed change stress. This study aimed to elucidate the impact of feed change stress and investigate the effect and mechanism of wheat oligopeptides (WOP) on the intestinal damage induced by feed change stress in broilers. A total of 120 one-d-old male Arbor Acre broilers (initial body weight [BW] 45.38 ± 0.64 g) were randomly allocated to two treatments (feed change or not) with 6 replicates of 10 birds, with monitoring for 60 h after changing feeds on d 11. A total of 240 one-d-old male Arbor Acre broilers (initial BW 45.33 ± 0.55 g) were randomly allocated to four treatments supplemented with graded levels of WOP (0.0, 0.1%, 0.2%, and 0.3%) with 6 replicates of 10 birds. The experimental period was 42 d. Compared with the no feed change (FC) group, broilers exhibited decreased feed intake after 4 h of changing feeds ( = 0.006), downregulated expression, upregulated and expression ( < 0.001), suppressed intestinal stem cell (ISC) differentiation evidenced by reduced , , , , and expression ( < 0.05). The stress induced by changing feeds in broilers may gradually diminish over time. Dietary WOP supplementation significantly improved growth performance of broilers. Compared with the control group, broilers fed diets supplemented with WOP showed higher BW at d 42 ( = 0.010), greater average daily gain (ADG) during d 11 to 42 ( = 0.010), and lower feed/gain ratio (F/G) during d 11 to 42 ( = 0.002), with 0.2% WOP being the optimal inclusion level. Mechanistically, WOP promoted ISC differentiation, partly by modulating the Wnt/β-catenin pathway, evidenced by upregulated , β-catenin, and mRNA and protein levels ( < 0.05). Notably, WOP counteracted feed change-induced suppression of nutrient transporters and inflammatory responses. These findings indicate that changing feeds impairs intestinal health via ISC dysregulation, while WOP alleviates these effects by modulating ISC differentiation and the Wnt/β-catenin signaling pathway. - Source: PubMed
Publication date: 2026/07/08
Fu YutongLu ZhengdaFang XinBianba CangjueShi XiaoyueCai QingheZhao YinuoHuang ShimengMa QiugangJi ChengZhao Lihong - Myocardial fibrosis is characterized by excessive cardiac fibroblasts (CF) proliferation and extracellular matrix deposition. The p53 tumor suppressor is known to inhibit CF proliferation, while the polycomb protein Bmi1 negatively regulates p53. Ellagic acid (EA), a natural polyphenol, has demonstrated anti-fibrotic potential, but its mechanism of action in the heart remains unclear. This study investigated whether EA reduces myocardial fibrosis by inhibiting Bmi1 expression. A rat model of myocardial fibrosis was established using isoproterenol (ISO), and rat cardiac fibroblasts were treated with TGF-β to induce a pro-fibrotic phenotype in vitro. Echocardiography and histology confirmed that EA treatment improved cardiac function and reduced fibrosis in ISO-induced rats. In vitro, EA significantly inhibited TGF-β-induced CF proliferation, migration, and differentiation into myofibroblasts. Mechanistically, EA upregulated p53 and its downstream target p21, leading to G1/S cell cycle arrest. Molecular docking and dynamics simulations predicted that EA binds to Bmi1, and subsequent experiments showed EA treatment reduced Bmi1 protein levels. Using a Bmi1 inhibitor (PTC-209) and overexpression plasmids, we demonstrated that the anti-fibrotic effects of EA are mediated in part through inhibition of Bmi1, which in turn activates the p53 pathway. Ellagic acid reduces myocardial fibrosis, at least in part, through suppression of Bmi1 expression. This suppression is associated with relief of the inhibitory effect of Bmi1 on p53, leading to p53/p21 pathway activation, cell cycle arrest, and subsequent inhibition of cardiac fibroblasts proliferation, migration, and differentiation. These findings suggest that Bmi1 may represent a novel therapeutic target for EA treatment of myocardial fibrosis. - Source: PubMed
Publication date: 2026/09/06
Li BolinShao ChongyuHuang XiaoxiaoZhou HuifenHuang KaiJin ChengsiWan HaiTong