Anti-ILK / Integrin-linked kinase, clone 3C7E1

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 (PubMed:8538749, PubMed:9736715). May act as a mediator of inside-out integrin signaling (PubMed:10712922). Focal adhesion protein part of the complex ILK-PINCH (PubMed:10712922). This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway (PubMed:10712922). Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells (PubMed:10712922). Regulates cell motility by forming a complex with PARVB (PubMed:32528174). Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B (PubMed:8538749, PubMed:9736715). [The UniProt Consortium]