F11r Antibody (OASA05167)
- Known as:
- F11r Antibody (OASA05167)
- Catalog number:
- oasa05167
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- F11r Antibody (OASA05167)
Related genes to: F11r Antibody (OASA05167)
- 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
Related products to: F11r Antibody (OASA05167)
Related articles to: F11r Antibody (OASA05167)
- Breast cancer (BC) is the most common cancer and the leading cause of cancer death among women worldwide. Its treatment is often ineffective due to metastasis in all BC subtypes and resistance to targeted therapy in HER2-positive breast cancer (HER2+ BC). On the other hand, the lack of traditional cell surface markers for molecularly targeted therapy in triple-negative breast cancer (TNBC) limits its treatment to conventional chemotherapy. Therefore, there is an urgent need to identify new molecular targets for BC therapy. The endothelial barrier, maintained by several types of cell junctions, including tight junctions (TJs), is loosened by cancer cells during the metastasis-linked processes. Cancer cells disrupt TJs in the endothelial wall of blood vessels and new TJs are formed between endothelial cells and cancer cells, leading to metastasis. The level of a TJ protein, F11 platelet receptor aka junctional adhesion molecule-A (F11R/JAM-A), is abnormal in most types of cancer, particularly in BC. The idea of targeting the F11R/JAM-A protein for BC treatment arose from the discovery that overexpression of the miR-145 microRNA in BC cells reduced F11R/JAM-A level and decreased cell migration. This observation was confirmed by subsequent studies, which supported the importance of F11R/JAM-A in cancer progression, particularly in BC. In this review, F11R/JAM-A is characterized as a molecular target for BC therapy. Particular attention was paid to peptide antagonists of F11R/JAM-A, that appear to be promising candidates for anticancer drugs. - Source: PubMed
Publication date: 2026/08/06
Bednarek RadosławŚwiątkowska Maria - HIV remains globally prevalent, and the long-term complications experienced by people living with HIV (PLWH) have increased interest in the functional heterogeneity of extracellular vesicle (EV) subpopulations. Defining these EV subsets may help clarify HIV-associated immune dysregulation and inform future diagnostic and therapeutic strategies. - Source: PubMed
Publication date: 2026/07/07
Ding NingSun JieweiZhu AiweiLi JiajunSun JinYan HongxiaMa YuanyuanHe XiangchuanZhang TongYao QiSu Bin - 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