MDC _ CCL22 (67 aa form) antigen
- Known as:
- MDC _ CCL22 (67 aa form) antigenic
- Catalog number:
- PA103X
- Product Quantity:
- 20
- Category:
- -
- Supplier:
- ACR
- Gene target:
- MDC _ CCL22 (67 form) antigen
Related genes to: MDC _ CCL22 (67 aa form) antigen
- Gene:
- CCL22 NIH gene
- Name:
- C-C motif chemokine ligand 22
- Previous symbol:
- SCYA22
- Synonyms:
- MDC, STCP-1, ABCD-1, DC/B-CK, A-152E5.1, MGC34554
- Chromosome:
- 16q21
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-22
- Date modifiied:
- 2016-10-05
Related products to: MDC _ CCL22 (67 aa form) antigen
'F 4_80 Antigen (mouse) Host Rat'F 4_80 Antigen (mouse) Host Rat(1R,2R,3R,5R)- 5-[(4-Methoxyphenyl)-diphenylmethylamino-6-bezyloxy-9H-purin-9-yl]-3-(phenylmethoxy)-2-[(phenylmethoxy)methyl]-cyclopentanol CAS: Form(2R,3R,5R)-3-(Benzyloxy)-5-(6-(benzyloxy)-2-(((4-methoxyphenyl)diphenylmethyl)amino)-1H-purin-9(6H)-yl)-2-((benzyloxy)methyl)cyclopentanone CAS: Form(Anti_Tg)Thyroglobulin Antigen(Des-Asp187)-Melanocyte Protein PMEL 17 (185-193) (human, bovine, mouse)
(Des-Asp187)-ME20M_ME20S (185-193) (human, bovine, mouse), (Des-Asp187)-Melanocyte Lineage-Specific Antigen GP100 (185-193) (hu(Des-Asp187,Met186)-Melanocyte Protein PMEL 17 (185-193) (human, bovine, mouse)
(Des-Asp187,Met186)-Melanoma-Associated ME20 Antigen (185-193) (human, bovine, mouse), (Des-Asp187,Met186)-95 kDa Melano(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Draxin) C1ORf187, Antigen blocking peptide(Val438)-Tyrosinase (432-444) (human)
(Val438)-LB24-AB (432-444) (human), (Val438)-Monophenol Monooxygenase (432-444) (human), (Val438)-SK29-AB (432-444) (human), (Val438)-Tumor Rejection Antigen AB ((αZ)-α-(Methoxyimino)-N-[(5aR,6R)-1,4,5a,6-tetrahydro-1,7-dioxo-3H,7H-azeto[2,1-b]furo[3,4-d][1,3]thiazin-6-yl]-2-furanacetamide CAS: 947723-87-7 Form0x19 Antigen Related articles to: MDC _ CCL22 (67 aa form) antigen
- Extranodal natural killer/T-cell lymphoma (ENKTL) is clinically characterized by destructive lesions that first appear in the nasal cavity and progress along the midline of the face. It was historically described as "rhinitis gangrenosa progressiva" or "lethal midline granuloma" due to its destructive clinical nature and had significant diagnostic and therapeutic challenges. This review synthesizes about 40 years of research, beginning with the 1980s and 1990s, when the disease was identified as a T-cell- or NK-cell-derived lymphoma, and the authors' discovery that clearly linked it to Epstein-Barr virus (EBV). ENKTL is highly prevalent in East Asia and characterized by a type II EBV latency pattern, in which the oncoprotein latent membrane protein 1 (LMP1) acts as a central driver of pathogenesis, activating critical signaling pathways including JAK/STAT, NF-κB, PI3K/Akt, and RAS/MAPK. These pathways, often bolstered by mutations in genes, trigger an oncogenic cascade involving epigenetic modifiers-enhancer of zeste homolog 2 (EZH2), histone deacetylase (HDAC). The deletion of chromosome 6q, leading to loss of function of tumor suppressor PR domain zinc finger protein 1 (PRDM1) and forkhead box O3 (FOXO3), as well as transcription of TNF α-induced protein 3 (TNFAIP3) and protein tyrosine phosphatase receptor type kappa (PTPRK), also contributes to pathogenesis. In vitro studies by the author's group demonstrated that autocrine/paracrine positive feedback loops involving several pro-proliferative molecules/cytokine/chemokine-CD27, ICAM1, hepatocyte growth factor (HGF), IL-9, IL-10, IL-15, CCL17, CCL22, CXCL10- further amplify ENKTL proliferation. Diagnostic precision has improved through the use of serum EBV DNA copy numbers and viral microRNAs (miRs), specifically miR-BART2-5p, alongside the emergence of soluble CD27 as a novel biomarker. While early anthracycline-based regimens failed due to multidrug resistance (MDR), modern concurrent chemoradiotherapy composed of MDR-independent drugs has significantly improved 5-year overall survival (OS) rates for localized disease to over 80%. For advanced or relapsed/refractory cases, L-asparaginase-based regimens are standard, though outcomes remain unsatisfactory. The therapeutic paradigm is currently shifting toward chemoradiotherapy combined with either immune checkpoint inhibitors or small-molecule drugs. Future research should focus on novel molecular-targeted therapies, immunotherapies, or combination strategies targeting proliferation-related molecules or LMP1. - Source: PubMed
Publication date: 2026/04/17
Harabuchi Yasuaki - Breast cancer derived extracellular vesicles (EVs) mediate tumor progression through surface protein-dependent intercellular communication; however, their molecular heterogeneity remains poorly characterized. In this study, we employed a proximity-dependent barcoding assay (PBA) together with patient-derived organoid (PDO) models and identified CDCP1 as a key driver of EV-mediated oncogenesis. PBA-based surface proteomics revealed CDCP1 as the most upregulated protein in breast cancer-derived EVs compared with EVs from normal tissues. Clinical validation confirmed elevated CDCP1 expression in tumor tissues and matched EVs. PDOs generated from fresh clinical specimens recapitulated CDCP1 expression levels of the parental tumors and secreted CDCP1-enriched EVs. Functional experiments showed that CDCP1-knockdown EVs suppressed PDO proliferation and sensitized tumors to chemotherapy. Mechanistically, CDCP1-positive EVs promoted macrophage polarization toward an M2 phenotype, accompanied by upregulation of IL-10 and TGF-β and CCL22. Multiplex immunofluorescence confirmed that CDCP1-high tumors exhibited increased co-localization of CD68⁺ and CD163⁺ macrophages. These results establish CDCP1 as a master regulator of EV driven breast cancer progression, linking surface proteome remodeling to chemo-resistance and immunosuppressive microenvironment reprogramming. The integration of single-EV profiling and PDO modeling establishes a translational framework for targeting CDCP1 as a promising therapeutic target and a candidate biomarker for future liquid biopsy development in aggressive breast cancer subtypes. - Source: PubMed
Publication date: 2026/04/13
Liu YibingMa LiZhu TingWu DiLiu Yonglei - CCL22 (macrophage-derived chemokine, MDC) is an important member of the CC chemokine family. By binding to its receptor CCR4, it regulates immune cell trafficking, plays a dual role in maintaining immune homeostasis and promotes immune-mediated inflammation. The biological effects of CCL22-CCR4 signaling in autoimmune diseases are highly dependent on the tissue microenvironment. Under steady-state conditions, CCL22 secreted by dendritic cells and macrophages recruits regulatory T-cells (Tregs) to peripheral tissues, suppresses excessive immune responses, and maintains immune tolerance. When CCL22 expression is down-regulated, Treg recruitment becomes insufficient, leading to immune dysregulation and tissue injury. CCL22 plays a critical role in the pathogenesis of several autoimmune diseases including vitiligo, systemic lupus erythematosus, and type 1 diabetes, although its biological effects vary across different disease contexts. This review focuses on the central roles of the CCL22-CCR4 axis in immune tolerance and inflammatory responses and describes how its functions are finely regulated by cell type, tissue microenvironment, and signaling states in different disease contexts. - Source: PubMed
Publication date: 2026/04/11
Zhang ZiXianMao HanXiaoXia ZhangRongLv XinYiHe YuanMin - Cancer immunotherapy has shown significant promise but faces challenges due to concerns around safety, the complex tumor microenvironment, and the low immunogenicity of cancer vaccines. Here, we report the synthesis of degradable chiral trimanganese tetroxide nanoparticles (MnO NPs) by modifying chiral mannose ligands to create chiral vaccines for cancer therapy and prevention. The L-type MnO nanoparticles (L-NPs) exhibit nearly twice the uptake rate into mouse bone marrow dendritic cells (BMDCs) compared to D-type MnO nanoparticles (D-NPs), thanks to a higher affinity for X-C motif chemokine ligand 1 (XCR1), cluster of differentiation 14 (CD14), and Toll-like receptor 4 (TLR4). When loaded with tumor antigens as vaccines (L-Vac), the L-NPs activate BMDCs through both NOD-like receptor protein 3 (NLRP3) inflammasome and cyclic GMP-AMP synthase-stimulator of interferon genes (cGAS-STING) pathways, enhancing the levels of C-C motif chemokine ligand 5 (CCL5) and reducing C-C motif chemokine ligand 22 (CCL22) expression. Molecular dynamics (MD) simulation explored the lock-and-key mechanism on the chiral NPs distinct patterns of interaction with antigen. Noticeably, the anti-tumor immunity was successfully confirmed in patient-derived xenograft (PDX) mouse model, depicting the clinical potential of chiral vaccines. L-Vac demonstrates high in vivo biosafety, breaking down into manganese ions that are primarily excreted through feces. Therefore, chiral adjuvants will pave a brilliant avenue to facilitate cancer immunotherapy. - Source: PubMed
Publication date: 2026/03/23
Chen PanpanWang WeiweiQu AihuaHua YihuiIerich Jéssica Cristiane Magalhãesde Moura André FariasXu LiguangKuang HuaXu ChuanlaiSun Maozhong - The chemokine system, comprising a network of chemokines and their receptors, orchestrates leukocyte migration and plays a central role in immune surveillance and inflammation. Targeting this system has emerged as a promising strategy in cancer immunotherapy and the treatment of immune-related disorders. C-C chemokine receptor 4 (CCR4), the receptor for chemokines CCL17 and CCL22, is a clinically validated therapeutic target for adult T cell leukemia/lymphoma, cutaneous T cell lymphoma, and other malignancies; however, the molecular mechanisms underlying CCR4 inhibition remain poorly understood. Here, we report five cryoelectron microscopy structures of human CCR4 in its apo state and in complex with four inhibitors. Tivumecirnon (FLX475) and Zelnecirnon (RPT193), two clinical-stage investigational drugs, bind to the orthosteric site of CCR4, blocking the chemokine recognition site 1. In contrast, AZD2098 and GSK2239633A occupy an allosteric site near the TM7-H8 turn, presumably interfering with G-protein coupling. Further analyses reveal that the therapeutic antibody mogamulizumab binds to the N-terminal region of CCR4 without competing with CCL17, suggesting that its antagonistic effect is mediated exclusively through antibody-dependent cellular cytotoxicity. Together, these structural insights elucidate distinct modes of CCR4 inhibition and provide a framework for the rational design of next-generation therapeutics targeting chemokine receptors. - Source: PubMed
Publication date: 2026/04/08
Zhou NingWang RongChen BaozhiQi Xiaofeng