ILK抗体

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     Black line: Control Antigen (100 ng); Purple line: Antigen(10ng); Blue line: Antigen (50 ng); Red line: Antigen (100 ng);    

  
  

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     Western blot analysis using ILK mouse mAb against Jurkat (1), NIH3T3 (2), HeLa (3), PC-12 (4), C6 (5), COS7 (6), Raji (7), K562 (8) and MCF-7 (9) cell lysate.    

  
  

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     Flow cytometric analysis of Jurkat cells using ILK mouse mAb (green) and negative control (red).    

  
  

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     Immunohistochemical analysis of paraffin-embedded human esophageal cancer tissues using ILK mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human rectum cancer tissues using ILK mouse mAb with DAB staining.    

  
  

Integrin-linked kinase (ILK) is a serine/threonine protein kinase that interacts with the cytoplasmic domain of integrin β subunits, serving as a critical adaptor between integrins and the actin cytoskeleton. Discovered in the mid-1990s, ILK plays a central role in regulating cell-matrix adhesion, migration, proliferation, and survival. It functions within focal adhesion complexes, mediating signaling crosstalk between integrins and growth factor receptors. ILK activity influences downstream pathways, including PI3K/Akt and Wnt/β-catenin, impacting processes like epithelial-mesenchymal transition (EMT) and apoptosis.

ILK antibodies are essential tools for studying its expression, localization, and function in both physiological and pathological contexts. Overexpression or dysregulation of ILK has been implicated in cancer progression, fibrosis, and cardiovascular diseases, making it a potential therapeutic target. Researchers use ILK-specific antibodies in techniques like Western blotting, immunohistochemistry, and immunofluorescence to assess protein levels in tissues or cultured cells. These antibodies also aid in exploring ILK's role in mechanotransduction and its interaction with binding partners like PINCH and Parvin. Validated ILK antibodies are commercially available, often distinguishing between phosphorylated and total protein forms to study activation states. Their application has advanced understanding of ILK's dual roles as a kinase and scaffolding molecule in development and disease.