F11R (Human) Recombinant Protein (P01)
- Known as:
- F11R (Human) Recombinant Protein (P01)
- Catalog number:
- H00050848-P01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- F11R (Human) Recombinant Protein (P01)
Related genes to: F11R (Human) Recombinant Protein (P01)
- Gene:
- BZW2 NIH gene
- Name:
- basic leucine zipper and W2 domains 2
- Previous symbol:
- -
- Synonyms:
- HSPC028, MST017, MSTP017
- Chromosome:
- 7p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-05
- Date modifiied:
- 2016-10-05
- Gene:
- C2CD3 NIH gene
- Name:
- C2 calcium dependent domain containing 3
- Previous symbol:
- -
- Synonyms:
- DKFZP586P0123
- Chromosome:
- 11q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2007-10-17
- Date modifiied:
- 2016-06-08
- Gene:
- F11R NIH gene
- Name:
- F11 receptor
- Previous symbol:
- JAM1
- Synonyms:
- PAM-1, JCAM, JAM-1, JAM-A, JAMA, CD321
- Chromosome:
- 1q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-10
- Date modifiied:
- 2016-10-05
- Gene:
- MBTD1 NIH gene
- Name:
- mbt domain containing 1
- Previous symbol:
- -
- Synonyms:
- SA49P01, FLJ20055
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-15
- Date modifiied:
- 2015-04-21
- Gene:
- TMEM63C NIH gene
- Name:
- transmembrane protein 63C
- Previous symbol:
- C14orf171
- Synonyms:
- DKFZp434P0111, CSC1, hsCSC1
- Chromosome:
- 14q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-10
- Date modifiied:
- 2017-10-17
Related products to: F11R (Human) Recombinant Protein (P01)
Related articles to: F11R (Human) Recombinant Protein (P01)
- Pancreatic islets respond to obesity-related insulin resistance by increasing β cell mass and insulin secretion. However, the molecular mechanisms behind this vital compensation are not fully understood. This study shows that adaptive islet-derived small extracellular vesicles (aid-sEVs) play a key role in β cell adaptation in obesity. Aid-sEV production rises under hyperlipidemic conditions, and uptake by adjacent cells occurs via F11R-mediated recognition. Mesenchymal stem cells (MSCs) act as downstream effectors after they internalize aid-sEVs, promoting β cell-adaptive responses. These vesicles deliver to MSCs, triggering dependent cellular reprogramming toward a Wnt-secreting phenotype. Restoration of in microRNA-deficient aid-sEVs restores their proadaptive effects on β cells. , a direct target of , is involved in regulating MSC proliferation and WNT secretion by controlling and transcription. These findings reveal a critical pathway controlling β cell compensation in diet-induced obesity and indicate that targeted enhancement of aid-sEV secretion could be a therapeutic strategy to counteract β cell dysfunction in diabetic patients. - Source: PubMed
Publication date: 2026/07/17
Guo XinweiWang YangDu RuixueYong WeiYan WenjingZhang ZichengPan YiZhang YanfengShen YumengYang YueZhang FangfangLiu JianxingTang WeiLiu YueJin Liang - Hirschsprung-associated enterocolitis remains a major postoperative complication of Hirschsprung's disease (HD), and impaired epithelial barrier integrity has been proposed as a contributing factor. In this study, we investigated whether 12-hydroxyheptadecatrienoic acid (12-HHT), an endogenous leukotriene B4 receptor 2 (BLT2) agonist, is associated with epithelial barrier enhancement and reduced inflammatory responses in patient-derived colonic organoids. - Source: PubMed
Publication date: 2026/07/16
Suda KazutoAbe KumpeiNishimura YurinaTanaka MasafumiNagasako YukiRao XuxuanZhang JianqinZeng SiyiFujiwara KentaroYamada ShunsukeIshii JunyaYoshida ShihoShibuya SoichiMiyano Go - Tight junctions are sites of cell-cell contacts at the apical region of epithelial junctions that are involved in barrier formation, cellular signaling, and cell-cell adhesion. Tight junctions are formed by integral membrane proteins associated with cytoplasmic scaffolding and adapter proteins through which they are linked to the underlying actomyosin and microtubule cytoskeletons. Here, we have addressed the interaction of the Junctional Adhesion Molecule (JAM)-C with the zonula adherens (ZO) protein ZO-2. Using a combination of cell-based recruitment assays and biochemical in vitro experiments, we find that JAM-C and ZO-2 directly interact in a PDZ domain-dependent manner. Notably, the interaction requires PDZ domain 3 as well as the SH3 domain of ZO-2, indicating that ZO-2 forms a functional supramodule to interact with JAM-C. We also found that JAM-C is specifically localized to tight junctions in polarized epithelial cells and that JAM-A suppresses JAM-C mRNA expression in these cells. Our findings have implications for important aspects of tight junction biology, including mechanosensing and liquid-liquid phase separation. - Source: PubMed
Publication date: 2026/06/10
Schulte AnnikaSchwietzer Mariel FBrinkmann FraukeTeuber ValentinCiti SandraFuruse MikioAurrand-Lions MichelEbnet Klaus - Furosemide (FSD) is a widely prescribed loop diuretic; however, its potential reproductive toxicity and its underlying mechanism have not been explored yet. The current study assessed the dose-dependent effects of FSD on testicular function in Sprague Dawley rats. Thirty-two male Sprague Dawley rats were apportioned into four groups i.e., control, FSD (10 mg/kg), FSD (20 mg/kg), and FSD (30 mg/kg) treated group. FSD exposure significantly downregulated the expression of blood-testis barrier genes (CLDN11, OCLN, TJP1, F11R, CDH2, GJA1), as well as upregulated pro-inflammatory mediators (NF-κB, TNF-α, IL-1β, IL-6, COX-2) in a dose-dependent manner, which indicates disruption of intercellular junctions and testicular inflammation. Oxidative stress was significantly increased, as revealed by increased ROS and MDA concentrations and decreased antioxidant enzymes (CAT, SOD, GPx, GSR, HO-1) after FSD exposure. Moreover, FSD intoxication suppressed the levels of reproductive hormones (LH and FSH, testosterone), indicating the impairment of the hypothalamic-gonadal axis. Apoptotic indices showed increased Bax, Caspase-3, Caspase-9 and decreased Bcl-2 after FSD administration, confirming activation of mitochondrial-mediated germ cell death. Similarly, semen analysis showed FSD exposure reduced the number, motility, sperm membrane integrity, and viability while increasing sperm abnormalities. Steroidogenic enzymes (StAR, 3β-HSD, 17β-HSD) were suppressed, which may indicate impaired biosynthesis of testosterone and spermatogenesis. Histopathological evaluations revealed severe degree of seminiferous tubule degeneration, reduction of germ cell population, and structure change of testicular architecture following the administration of FSD. Collectively, these findings demonstrate the multifaceted testicular toxicity of FSD, via disruption of BTB, oxidative stress, hormonal dysregulation, apoptosis and structural degeneration, leading to eventual consequences on male reproductive health. These results distinguish the potential reproductive risk caused by FSD exposure, warranting clinical trials for validation in humans. - Source: PubMed
Publication date: 2026/06/01
Aloraini Ghfren SAlissa MohammedAlghamdi Abdullah - BackgroundIntegrated bioinformatics approaches were used to identify stage-specific candidate genes and potential drug targets in triple-negative breast cancer (TNBC).MethodsMicroarray (164 early-stage, 33 advanced-stage, and 53 normal samples) and RNA-seq (113 normal, 163 early-stage, and 30 advanced-stage TNBC samples) datasets were analyzed. Differentially expressed genes (DEGs) were identified, followed by co-expression analysis using Weighted Gene Co-expression Network Analysis (WGCNA) and protein-protein interaction analysis using the STRING database. miRNA co-regulation was evaluated using multiMiR and TCGA correlation analyses. Candidate genes were validated using UALCAN and immunohistochemistry data. Molecular docking assessed potential therapeutic agents.ResultsNovel stage-specific candidate biomarkers were identified, including , , , and in early-stage TNBC, and , , , and in advanced-stage TNBC. UALCAN analysis confirmed the dysregulation of these genes across 23 additional malignancies. STRING-based network analysis revealed stage-specific protein-protein interactions, including SKP2-SKP1 in early-stage and F11R-TJP1 in advanced-stage TNBC. miRNA co-regulation distinguished early-stage TNBC through PI3K-AKT-related pathways and advanced-stage TNBC through tumor progression-associated pathways. Docking-based drug repurposing highlighted conventional agents (e.g., doxorubicin) and potential novel candidates (e.g., sunitinib).ConclusionThis study identifies novel stage-specific gene candidates and suggests repurposable drugs for TNBC, supporting progression-specific targeted therapeutic strategies. - Source: PubMed
Publication date: 2026/05/28
Shahraki FaezeMeshkini AzadehNazari Elham