Anti-Integrin linked kinase (ILK)

0.5mg/ml if reconstituted with 0.2ml sterile DI water. ILK, also known as Integrin-linked kinase, is a serine-threonine protein kinase. Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK) interacts with the cytoplasmic domain of beta-1 integrin. This gene was initially described to encode a serine/ threonine protein kinase with 4 ankyrin-like repeats, which associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. Recent results showed that ILK contains 5 ankyrin-like repeats, and that the C-terminal kinase domain is actually a pseudo-kinase with adaptor function. Protein function: 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 beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B. [The UniProt Consortium]