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 encodes 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. [provided by RefSeq, Jul 2008].
custom-made
ILK
Spezies: Maus
Wirt: HEK-293 Cells
Recombinant
> 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
custom-made
ILK
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
> 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
custom-made
ILK
Spezies: Maus
Wirt: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
WB, ELISA, SDS
custom-made
ILK
Spezies: Human
Wirt: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
WB, ELISA, SDS
Radovanac, Morgner, Schulz, Blumbach, Patterson, Geiger, Mann, Krieg, Eckes, Fässler, Wickström: "Stabilization of integrin-linked kinase by the Hsp90-CHIP axis impacts cellular force generation, migration and the fibrotic response." in: The EMBO journal, Vol. 32, Issue 10, pp. 1409-24, (2013) (PubMed).