Human Polyclonal EpCAM Ab
- Known as:
- Human Polyclonal EpCAM Antibody
- Catalog number:
- a0895
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- ABclonal
- Gene target:
- Human Polyclonal EpCAM
Related genes to: Human Polyclonal EpCAM Ab
- Gene:
- EPCAM NIH gene
- Name:
- epithelial cell adhesion molecule
- Previous symbol:
- M4S1, MIC18, TACSTD1
- Synonyms:
- Ly74, TROP1, GA733-2, EGP34, EGP40, EGP-2, KSA, CD326, Ep-CAM, HEA125, KS1/4, MK-1, MH99, MOC31, 323/A3, 17-1A, TACST-1, CO-17A, ESA
- Chromosome:
- 2p21
- Locus Type:
- gene with protein product
- Date approved:
- 1995-10-02
- Date modifiied:
- 2019-04-23
Related products to: Human Polyclonal EpCAM Ab
Related articles to: Human Polyclonal EpCAM Ab
- Mismatch repair-deficient (dMMR) sarcomas are rare and incompletely characterized. Here, we studied 39 sarcomas with high microsatellite instability (MSI-H) and/or biallelic MMR gene inactivation (21 MSH2, 9 MLH1, 4 PMS2, 4 MSH6, 1 EPCAM). All tumors evaluated with immunohistochemistry (IHC; n = 36) showed loss of MMR protein expression. Eight sarcomas were index neoplasms among the 15 patients with documented Lynch syndrome. Eighteen of 1531 sarcomas (1.2%) in our sequencing database were dMMR, with enrichment in pleomorphic rhabdomyosarcoma (PRMS; 1/5), uterine leiomyosarcoma (LMS; 7/124; 5.6%), and unclassified/undifferentiated pleomorphic sarcoma (UPS; 6/259; 2.3%). MMR IHC screening of independent cases confirmed MMR deficiency in PRMS (2/20), uterine LMS (2/20), and unclassified/UPS (1/20). Two histologic patterns were identified among unclassified/UPS. Ten tumors, designated "distinctive lobulated inflammatory sarcoma" (DLIS), showed lobular architecture, florid inflammation, and histiocytoid, variably pleomorphic neoplastic cells. All 6 patients with DLIS and follow-up (median: 6.0 y; range: 3 mo to 8.6 y) were alive with no evidence of disease (ANED), and 2 DLIS responded completely to immune checkpoint inhibition. A morphologically different group of 6 unclassified high-grade sarcomas showed sheets of epithelioid-to-rhabdoid cells with eosinophilic cytoplasm; among 5 patients with follow-up (median: 1.1 y; range: 4 mo to 6.9 y), only 1 was ANED. Surprisingly, all 3 PRMS patients with follow-up (median: 5.7 y; range: 4.2 to 8.3 y) were ANED, including 2 with complete responses of metastases to systemic therapy. We conclude that PRMS, uterine LMS, and unclassified/UPS showed sufficiently prevalent MMR deficiency to justify prospective MMR IHC screening for Lynch syndrome and to identify patients who might benefit from immune checkpoint inhibition. Histologic subtyping of unclassified sarcomas predicted prognosis and therapeutic response. We propose universal MMR IHC screening of (1) PRMS, (2) uterine LMS, (3) unclassified/UPS, and (4) any sarcoma in a patient with a personal or family history of Lynch syndrome. - Source: PubMed
Publication date: 2026/06/12
Odintsov IgorNowak Jonathan ABaranov EstherAlcindor ThierryHaddox Candace LVenkataraman VinayakSholl Lynette MGeorge SuzanneDoyle Leona ARedston MarkPapke David J - Tumor cell migration relies on the integration of extracellular matrix (ECM) remodeling, cell surface signaling regulating cytoskeleton dynamics, and epithelial-to-mesenchymal transition (EMT). Clusterin (CLU), a secreted glycoprotein, is involved in extracellular proteostasis and is known to interact with members of the LDL receptor family, including low-density lipoprotein receptor-related protein 1 (LRP1). Beyond its canonical chaperone activity, CLU is involved in several biological processes, including cell survival, apoptosis, tissue remodeling, inflammation and cancer progression. On the other hand, the membrane type 1 matrix metalloproteinase (MT1-MMP), functionally linked to CD44 and LRP1, represents a key membrane-associated molecule that may control cell adhesion and receptor-mediated uptake of ECM ligands and proteases. In this article, we critically highlight a hypothetical model in which secreted CLU (sCLU) may function as the central player of a dynamic membrane-associated network integrating proteolysis, endocytosis, and intracellular signaling. Based on recent literature findings and STRING analyses, LRP1, MT1-MMP, CD44, and cell surface matrix components, such as proteoglycans (PGs) and integrins, are likely to be involved. By coordinating this membrane-associated molecular crosstalk, sCLU may integrate ECM remodeling with cytoskeletal dynamics and EMT-related programs related to invasive behavior. Overall, this framework highlights a potential mechanism through which sCLU may contribute to tumor cell plasticity and aggressiveness, suggesting new avenues for therapeutic intervention. - Source: PubMed
Publication date: 2026/05/30
Ciringione AlessiaRizzi FedericaMangani SylviaPiperigkou ZoiKaramanos Nikos - Immune escape is a hallmark of lung cancer, and limited responsiveness to PD-1/PD-L1 blockade highlights the need to identify additional immunoregulatory mechanisms in the mediastinal tumor microenvironment (TME). Non-classical immune checkpoints, including CD137/CD137L and CD200/CD200R, may interact with classical pathways but remain insufficiently defined in metastatic lymph nodes (LNs). We evaluated their expression on tumor cells and lymphocytes and their associations with PD-L1 and PD-L2. - Source: PubMed
Publication date: 2026/05/26
Kwiecień IwonaRaniszewska-Borys AgataRutkowska ElżbietaSokołowski RafałJahnz-Różyk KarinaRzepecki Piotr - CD3 T cell engagers (TCEs) have transformed hematologic oncology, but dose-liming toxicity and the absence of adequate costimulation have limited TCE success in solid tumors. Consequently, to date, only one classical TCE developed for solid tumors - tarlatamab - has been granted a marketing approval. Here, we report a pioneer combination strategy using a novel CD2-targeted costimulatory bispecific antibody to overcome these limitations. Building on a unique non-blocking CD2 antibody, we developed a HER2×CD2 proof-of-concept bispecific that, combined with an EpCAM×CD3 TCE, provides tumor-dependent costimulation and enhances anti-tumor cytotoxicity mediated by the TCE. We show that HER2×CD2 can be dosed independently to restore optimal anti-tumor cytotoxicity of a sub-efficacious low dose of the EpCAM×CD3 TCE, thus providing a route to avoid TCE-driven toxicity while maintaining efficacy. In a humanized xenograft model, co-treatment with HER2×CD2 achieved complete tumor remission in 8 of 9 mice at a TCE dose that otherwise mediated complete remission in only 1 of 9 mice. We show that HER2×CD2 compensates for the loss of CD58 expression by tumor cells - a well-documented tumor escape mechanism. Notably, unlike CD28-based costimulation, HER2×CD2 effectively also harnessed the anti-tumor cytotoxicity of CD28-negative CD8 T cells - a potent cytotoxic subset prevalent in elderly patients and dominant in solid tumors. Furthermore, HER2×CD2 induced markedly lower cytokine release than a HER2×CD28 bispecific while mediating comparable improvement in anti-tumor cytotoxicity. These findings establish our novel CD2-targeted costimulatory bispecific antibody approach as a promising and potentially safe way to expand and enhance TCE immunotherapy for solid tumors. - Source: PubMed
Publication date: 2026/06/10
Danquah WelbeckPichery MélanieEden ThomasBoyance AurelienPasquet LiseRoure VirginieMars MarionMarchand AliceGumz EllenGador MylèneValente LouContini MarionCzernecki LukasShanmuganathan SanjithBarron PaulineChabot SophieDangl MarkusNiederfellner Gerhard - 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