Integrins are transmembrane receptors that mediate cell-cell or cell-matrix adhesion. All integrins are heterodimers composed of α and β subunits, which interact with extracellular matrix and cytoskeletal proteins. Signal transduction through intergin receptors may be regulated by integrin-linked kinase (ILK). ILK is a widely expressed Ser/Thr protein kinase that contains four ankyrin-like repeats in the N-terminal region, a phoshoinositide lipid-binding motif at amino acids 180-212, and an integrin binding site at amino acids 293-451. The ankyrin repeats interact with a LIM domain-only protein called PINCH that also binds the adaptor protein, Nck-2. This interaction implicates ILK in growth factor receptor pathways. In addition, the interaction of ILK with the cytoplasmic domains of integrin β1 and β3 subunits and localization of ILK to focal adhesion plaques suggests a role for ILK in the regulation of cell adhesion. Interestingly, overexpression of ILK in epithelial cells inhibits cell adhesion and stimulates cell cycle progression and tumorigenicity. Thus, ILK regulates signal transduction in many different cell signaling pathways.
Host Species: Mouse
Species Reactivity [for Features Main]: Human
Immunogen: Human ILK aa. 326-452
Immunofluorescence, Western Blotting
|Human ILK aa. 326-452|
|Store undiluted at -20°C.|
|Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.|
For Research Use Only.
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