Anti-Human CD82 FITC 25 tests
- Known as:
- Antibody toHuman CD82 fluorecein 25 tests
- Catalog number:
- 11-0829-41
- Category:
- -
- Supplier:
- eBioscience
- Gene target:
- Anti-Human CD82 FITC 25 tests
Related genes to: Anti-Human CD82 FITC 25 tests
- Gene:
- CD82 NIH gene
- Name:
- CD82 molecule
- Previous symbol:
- ST6, KAI1
- Synonyms:
- R2, IA4, TSPAN27
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-10
- Date modifiied:
- 2017-07-28
Related products to: Anti-Human CD82 FITC 25 tests
Related articles to: Anti-Human CD82 FITC 25 tests
- Tetraspanin CD82/KAI1 inhibits cell movement and metastasis of malignant tumors, and reduced and lost expressions of CD82 predict worse outcomes of patients with malignant tumors. Here we found that CD82 inhibits both solitary and collective movement of tumor cells. The CD82 YVAA mutation, which affects CD82 trafficking, selectively abrogates CD82-mediated inhibition of collective migration. Cilengitide, at the concentration that specifically inhibits integrin αVβ3, also selectively blocks collective movement, underscoring a promotive role of integrin αVβ3 in this mode of cell motility. In contrast, integrin αVβ5 appears non-essential for collective migration, and both αVβ3 and αVβ5 are dispensable for solitary movement on fibronectin, highlighting distinct functions of different integrins in different modes of tumor cell movement. CD82 interacts with αVβ3 and αVβ5 integrins and downregulates their protein levels, while CD82 YVAA mutation relinquishes this downregulation without disrupting CD82 interactions with these integrins. Mechanistically, CD82, but not the YVAA mutant, considerably reduces digitation junction-the structure where integrin αVβ3 localizes-and likely directs integrin αVβ3 for lysosomal degradation, thereby lowering its level and suppressing collective migration. Thus, our study reveals that i) integrin αVβ3 promotes collective movement of tumor cells, ii) CD82 counteracts this by diminishing integrin αVβ3 and its presence in microextrusions, and iii) digitation junction likely participates in collective cell movement. Our study further demonstrates that endolysosomal trafficking of CD82 and integrin αVβ3 is needed for their collective movement-regulatory activities and that coupling of metastasis suppressor CD82/KAI1 with different partners regulates different modes of cell movement. - Source: PubMed
Publication date: 2026/06/22
Wang Xue JunRichardson Mekel MDing YingjunJiang ChaoLiu SonglanZhou BinLi ShupingChen JunxiongRubinstein EricHays Franklin AMehla KamiyaZhang Xin A - Benign airway stenosis (BAS) involves progressive pathological narrowing of the trachea and main bronchi, causing clinically significant respiratory impairment that can advance to life-threatening obstruction. While fibrosis arises from dysregulated immune-stromal crosstalk, the specific cellular and molecular drivers of BAS remain poorly understood. - Source: PubMed
Publication date: 2026/06/16
Liu YifeiJing LeiLuo YukaiChen LuyangJia Qing-ChunChen XiaohuiChen ShaohuaZhang HuapingCheng WenzhaoZhou YunzhiZeng Yiming - KITENIN (KAI1 C-terminal interacting tetraspanin) has emerged as a critical oncogenic mediator involved in tumor initiation, progression, metastasis, and therapeutic resistance. Initially identified through its interaction with the metastasis suppressor KAI1/CD82, KITENIN activates c-Jun N-terminal kinase (JNK) signaling and AP-1-dependent transcription, thereby driving epithelial-mesenchymal transition (EMT), cytoskeletal remodeling, and invasive behavior. Aberrant KITENIN expression has been reported in diverse solid tumors, including colorectal, gastric, hepatocellular carcinomas, and glioblastoma, where it correlates with aggressive phenotypes and poor prognosis. Preclinical studies show that genetic knockdown or pharmacological inhibition of KITENIN reduces metastatic potential and restores sensitivity to chemotherapy, underscoring its therapeutic relevance. Beyond metastasis, KITENIN contributes to cancer stemness, immune evasion, and resistance to conventional treatments, positioning it as a multifaceted regulator of tumor biology. Recent efforts to therapeutically target KITENIN include small molecules, natural compounds, and peptide-based inhibitors, though clinical translation remains in early stages. This review outlines the structural and mechanistic underpinnings of KITENIN-driven oncogenesis, evaluates its prognostic significance, and consolidates emerging evidence on KITENIN-targeted approaches. By highlighting current gaps and future directions, we propose that targeting the KITENIN axis holds promise for suppressing metastasis and improving outcomes in precision oncology. - Source: PubMed
Publication date: 2026/05/19
Salam S M AbdusJahan EshratBae Jeong AAhn Eun-JungKim Sung JinLee Kyung-HwaMoon Kyung-SubKim Kyung Keun - Epidermal growth factor receptor (EGFR) regulates cell growth, differentiation, and migration through mechanisms of ligand binding and dimerization. Tetraspanin CD82 is known to interact with and regulate EGFR; however, the underlying molecular mechanisms are not clear. In this study, we used detergent-solubilized and detergent-purified EGFR-CD82 complexes and fusion proteins to characterize the interaction of EGFR with CD82 by size-exclusion chromatography and cryo-electron microscopy. Our data show that CD82 binds monomeric EGFR and dissociates from EGFR dimers. Congruently, less EGF is bound to EGFR in the presence of CD82, likely because of reduced EGFR dimerization. AlphaFold2 multimer predictions together with a 15 Å resolution cryo-EM density map support a curved-back conformation of EGFR with a putative interaction site between monomeric EGFR domain IV and the large extracellular loop of CD82. Together, our results support CD82 regulating EGFR function by hindering dimer formation and show CD82 dissociation from EGFR upon EGF-induced EGFR dimerization. - Source: PubMed
Publication date: 2026/05/13
Lamottke ElisaBrondijk T Harma CGros Piet - Transfer RNA-derived small RNAs (tsRNAs), a recently identified class of non-coding RNAs, have been shown to play regulatory roles in various malignancies. However, their functions in lung adenocarcinoma (LUAD) remain largely unexplored. This study aims to elucidate the molecular mechanisms and biological functions of tRF-24-O7M8LO9LIM in LUAD. Quantitative reverse transcription polymerase chain reaction (qRT-PCR) was used to measure the expression levels of tRF-24-O7M8LO9LIM in LUAD patient tissues and lung cancer cell lines. Chi-square tests were performed to analyze the correlations between its expression and clinicopathological characteristics. Kaplan-Meier survival analysis was conducted to assess its prognostic significance. Plasmids for the knockdown and overexpression of tRF-24-O7M8LO9LIM were constructed, and their effects were validated through in vitro cell-based assays-including CCK-8, EdU, colony formation, and Transwell assays-as well as in vivo tumorigenicity experiments in nude mice. A dual-luciferase assay was employed to validate the relationship between tRF-24-O7M8LO9LIM and its downstream target genes. KEGG pathway analysis and western blotting were further used to validate the associated signaling pathways. The results showed that tRF-24-O7M8LO9LIM is highly expressed in LUAD patient tissues and lung cancer cells, correlates with TNM stage and tumor size, and has significant prognostic value. Knockdown of tRF-24-O7M8LO9LIM inhibited cellular proliferation, migration, and invasion in vitro, while simultaneously suppressing tumor growth in vivo. The dual-luciferase assay confirmed the direct binding between tRF-24-O7M8LO9LIM and its downstream target, CD82. KEGG pathway analysis and western blotting experiments demonstrated that tRF-24-O7M8LO9LIM regulates the p53 signaling pathway via CD82. In conclusion, tRF-24-O7M8LO9LIM promotes the progression of LUAD by targeting CD82 to regulate the p53 signaling pathway. - Source: PubMed
Publication date: 2026/04/15
Liu SinanZhu KuiWu YixuanChu FuyingZhao PingZhou LiningWu AnqiChen Xiang