Anti-Mouse CD66a (CEACAM1) PE 25 ug
- Known as:
- Antibody toMouse CD66a (CEACAM1) PE 25 ug
- Catalog number:
- 12-0661-80
- Category:
- -
- Supplier:
- eBioscience
- Gene target:
- Anti-Mouse CD66a (CEACAM1) 25
Related genes to: Anti-Mouse CD66a (CEACAM1) PE 25 ug
- Gene:
- CEACAM1 NIH gene
- Name:
- carcinoembryonic antigen related cell adhesion molecule 1
- Previous symbol:
- BGP
- Synonyms:
- BGP1, CD66a
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2016-01-14
Related products to: Anti-Mouse CD66a (CEACAM1) PE 25 ug
Related articles to: Anti-Mouse CD66a (CEACAM1) PE 25 ug
- Immune checkpoint blockade (ICB) therapies, particularly antibodies blocking, the programmed cell death protein 1 (PD-1)/programmed cell death-ligand 1 (PD-L1), have shown clinical success but remain limited by suboptimal response rates, often due to insufficient immune activation. T-cell immunoglobulin and mucin domain-containing protein-3 (TIM-3), a non-redundant immune checkpoint frequently co-expressed with PD-1, drives severe T-cell exhaustion in solid tumors and contributes to resistance against anti-PD-1/PD-L1 therapy. Thus, dual blockade of TIM-3 and PD-1 may restore more effective anti-tumor immunity. Compared to antibodies, low-molecular-weight peptides offer advantages in combination therapy, including better tissue penetration, lower immunogenicity, improved tolerability and low production costs. Cyclic peptides, in particular, provide enhanced biological activity and proteolytic stability. Here, we present TBP1, a cyclic peptide identified via a bacterial surface display library, which binds TIM-3 with high affinity and specificity. Competitive blocking assays and molecular docking confirmed that TBP1 effectively disrupts TIM-3 interactions with Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM-1) and Phosphatidylserine (PtdSer). In vitro, TBP1 restored exhausted T-cell function by disrupting the TIM-3/CEACAM-1 interaction. In CT26 tumor-bearing mice, TBP1 synergized with an anti-PD-1 antibody, enhancing anti-tumor immunity by promoting CD4 T cell infiltration and IL-2 secretion. These findings identify TBP1 as a novel TIM-3-targeting cyclic peptide and support its potential application in combination immune checkpoint blockade. - Source: PubMed
Publication date: 2026/09/02
Huang YingLi JialeQin YingzhouQie BoWang QianqianLiu CuijuanZhu Yimin - Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is an inhibitory receptor expressed by multiple tumors, including colorectal cancer (CRC). CEACAM1 exists as a long isoform (L) containing immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and a short isoform (S) lacking ITIMs. While microsatellite instability (MSI) CRCs respond to immunotherapy, microsatellite-stable (MSS) CRCs remain resistant, highlighting the need for alternative therapeutic targets. We previously developed an agonistic anti-CEACAM1 monoclonal antibody (mAb), CCM5.01, and demonstrated its CEACAM1-dependent inhibitory effects in melanoma. Here, we evaluated CCM5.01 inhibitory activity on CRC cell lines and related it to L/S ratio. - Source: PubMed
Publication date: 2026/08/31
Niazov ShiranZaffran IlanBenny OfraBen-Zimra MichaLevi-Schaffer Francesca - Hypervirulent Klebsiella pneumoniae (hvKp) infection often induces sepsis characterised by remarkable phenotypic and functional diversity among neutrophils. However, the roles of distinct lung neutrophil compartments involved in hvKp infection remain poorly understood. Here, utilising single-cell RNA sequencing, we identified four neutrophil subsets in the lungs of hvKp-infected mice: N1, N2, N3a, and N3b, which were organised along a maturation trajectory. Functionally, early-stage subsets exhibited proinflammatory and phagocytic activities with high levels of activation, whereas terminal subsets displayed enhanced pathogen sensing and immunoregulatory properties. Notably, the N3b population showed pronounced immunosuppressive features and was predicted to inhibit lymphocyte responses through Lgals9 and Ceacam1 ligands, potentially associated with hvKp-induced lymphopenia. Projection onto NeuMap further validated the functional states of identified subsets, linking N1 to proliferative programmes, N2 to granules and hypoxia-associated metabolic activity, N3a to antigen-presentation signatures and N3b to immunosuppressive hubs. Morphologically, N3a/b were predicted to be enriched for segmented neutrophils, consistent with a more mature phenotype compared with N1 and N2. Notably, segmented neutrophils were markedly expanded in infected lungs, suggesting their association with hvKp pathogenesis. Together, our findings delineate the lung neutrophil landscape in hvKp-induced sepsis, providing insights for understanding hvKp pathogenesis and developing targeted therapeutic interventions at a neutrophil subset level. - Source: PubMed
Publication date: 2026/08/27
Fang XiangLi WeizhaoZhang XinyuMina Sohana AkterJiang QianlingZhu GaochenChen ShengYang Guan - CEACAM1 homodimerization mediates tumor immune evasion, presenting a compelling target to overcome resistance to PD-1 blockade. However, defining a precise structural and pharmacological blueprint for CEACAM1 targeting has remained challenging. Here, we report the discovery and comprehensive preclinical characterization of MG1124, a highly specific, fully human monoclonal antibody targeting the CEACAM1 IgV domain. X-ray crystallographic analysis at a 1.8 Å resolution revealed that MG1124 binds the homodimerization interface with robust affinity (KD = 37.8 nM), physically disrupting both homophilic and heterophilic inhibitory interactions without cross-reacting with highly homologous CEACAM members. This targeted structural blockade effectively reversed CEACAM1-mediated suppression of T-cell receptor signaling, restoring ZAP70 phosphorylation and IL-2 production, while potently enhancing NK- and CD8⁺ T-cell cytotoxicity against CEACAM1-high tumor cells. In vivo, MG1124 reprogrammed the tumor immune microenvironment by increasing effector cytokine production in human CEACAM1 knock-in mice. It also demonstrated robust tumor growth inhibition in humanized non-small cell lung cancer (NSCLC) patient-derived xenograft (PDX) models, synergizing profoundly with PD-1 blockade. Furthermore, multiplex immunofluorescence profiling of human NSCLC tissues confirmed robust CEACAM1 expression across tumor and immune compartments, reinforcing its translational validity. Finally, MG1124 exhibited a highly favorable, drug-like pharmacokinetic profile in cynomolgus monkeys, characterized by prolonged systemic exposure and low clearance. By defining the structural basis of CEACAM1 blockade and demonstrating translational efficacy, this study introduces MG1124 as a novel therapeutic antibody, providing a robust pharmacological foundation for cancer immunotherapy. - Source: PubMed
Publication date: 2026/08/27
Lee Jae-ChulOh MiyoungNam Hye-MiCho Hyun-JungKim Jae HwanCho Byoung ChulKim SeonghoonOh Byung-HaLee Chang-Woo - Natural killer (NK) cells are active tumoricidal cells that inhibit esophageal cancer (EC) development, making them a prospective immunotherapeutic tool. Nonetheless, NK cells undergo both activation and exhaustion in the tumor microenvironment, but the related mechanisms have not been thoroughly understood. Using a chemical-induced EC model, we investigated the expression pattern and functional properties of zinc finger protein 600 (ZNF600) in EC-associated NK cells. For the first time, we revealed that ZNF600 expression was diminished in EC-associated NK cells, particularly those exhibiting the exhaustion phenotype. In vitro silencing of ZNF600 resulted in a remarkable downregulation of tumor necrosis factor (TNF), interferon-gamma (IFN-γ), and cytolytic perforin and granzyme B, leading to an impairment of NK cell tumoricidal capacity. On the contrary, ZNF600 overexpression promoted NK cell tumoricidal capacity. Adoptive transfer of ZNF600-overexpressing NK cells significantly inhibited the growth of EC implants. Furthermore, EC cells significantly down-regulated ZNF600 in NK cells. Interestingly, neutralizing carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) and T cell immunoglobulin and mucin-domain containing-3 (TIM-3) partially restored ZNF600 expression after co-culture with EC cells. Conclusively, the CEACAM1-TIM-3 signaling axis might decrease ZNF600 in EC-associated NK cells and subsequently suppress NK cell-mediated killing of EC cells. This research discovers a novel mechanism by which the EC microenvironment induces NK cell dysfunction. - Source: PubMed
Publication date: 2026/08/26
He JiongmingLiu ShanWang LingyingXiong Fei