ITGA3抗体—艾普蒂

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     Western blot analysis using NPM mouse mAb against SMMC-7721 (1), HepG2 (2), Hela (3) and HEK293 (4) cell lysate.    

  
  

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     Confocal Immunofluorescence analysis of Hela (left) and NTERA-2 (right) cells using NPM mouse mAb (green). Red: Actin filaments have been labeled with DY-554 phalloidin.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human liver carcinoma tissues, showing nuclear localization using NPM mouse mAb with DAB staining.    

  
  

The ITGA3 antibody targets the integrin alpha-3 (ITGA3) subunit, a critical component of the α3β1 integrin heterodimeric receptor. Integrins are transmembrane proteins that mediate cell-cell and cell-extracellular matrix (ECM) interactions, regulating processes like adhesion, migration, proliferation, and survival. ITGA3 pairs with β1 (ITGB1) to form a receptor for laminin, fibronectin, and other ECM ligands, playing roles in tissue development, wound healing, and epithelial cell function. Dysregulation of ITGA3 is implicated in pathological conditions, including cancer metastasis, fibrosis, and inflammatory disorders. In cancer, elevated ITGA3 expression correlates with tumor invasion, angiogenesis, and poor prognosis, as it facilitates ECM remodeling and signaling through pathways like PI3K/AKT and MAPK.

ITGA3 antibodies are widely used in research to study integrin-mediated mechanisms in vitro and in vivo. They enable detection of ITGA3 expression via techniques like Western blotting, immunofluorescence, and flow cytometry, aiding in biomarker discovery. Function-blocking ITGA3 antibodies help elucidate its role in cell-ECM interactions by inhibiting ligand binding or downstream signaling. Therapeutic potential is also being explored, with antibody-based strategies aiming to disrupt integrin-driven pathways in diseases like metastatic cancers. These antibodies are typically monoclonal, derived from mice or rabbits, and validated for specificity across applications. Research on ITGA3 continues to advance understanding of integrin biology and its translational relevance.