An E.coli-derived zebrafish Integrin-linked kinase recombinant protein (amino acids M1-H203) was used as the immunogen for the Zebrafish Integrin-linked kinase antibody.
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.
