ILK1 Recombinant Protein

Source : Escherichia Coli. ILK1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 452 amino acids fragment (1-452) having a molecular mass of 55.92kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The ILK1 is purified by proprietary chromatographic techniques. ILK1 (Integrin-linked kinase) is a serine/threonine protein kinase, containing 4 ankyrin-like repeats. ILK1 regulates a number of biological properties which include: anchorage-independent cell cycle progression, tumor cell invasion and apoptosis. ILK1 can also be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Furthermore, ILK1 phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.ILK1 interacts with the cytoplasmic domains of integrin 1 and 3 subunits in addition to several adaptors and signaling proteins, it also acts as a proximal receptor kinase regulating integrin-mediated signal transduction. ILK1 is a focal adhesion protein part of the complex ILK-PINCH. This complex is deemed to be one of the convergence points of integrin- and growth factor-signaling pathway. ILK1 is stimulated rapidly but briefly by both cell fibronectin interactions, as well as by insulin, in a PI3-K-dependent manner, probably through the binding of PtdIns (3,4,5) P3 with a PH-like domain of ILK.ILK1 over-expression has been documented in a wide variety of human malignancies.