anti-ILK, pAb

Integrin-linked kinase (ILK) is an adaptor and signaling protein that couples integrins to the actin cytoskeleton and coordinates signal transduction from extracellular matrix and growth factors. By interacting with the focal adhesion proteins PINCH, paxillin, and parvin, ILK regulates integrin-mediated cell adhesion and cytoskeletal dynamics within focal adhesions to regulate cell adhesion, spreading, and migration. ILK is involved in the suppression of apoptosis and promotion of cell survival through the phosphorylation of AKT (Ser473), GSK-3 (Ser9), myosin light chain (Ser18/19), and affixin. ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN. Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates β-1 and β-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.