|Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Zebrafish|
Application Methods: Immunoprecipitation, Western Blotting
Background: Integrin-linked kinases (ILKs) couple integrins and growth factors to downstream pathways involved in cell survival, cell cycle control, cell-cell adhesion and cell motility (1). ILK functions as a scaffold bridging the extracellular matrix (ECM) and growth factor receptors to the actin cytoskeleton through interactions with integrin, PINCH (which links ILK to the RTKs via Nck2), CH-ILKBP and affixin (1). ILK phosphorylates Akt at Ser473, GSK-3 on Ser9, myosin light chain 2 (MLC2) on Ser18/Thr19, as well as affixin (2-5). These phosphorylation events are key regulatory steps in modulating the activities of the targets. ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN and a PP2C protein phosphatase, ILKAP (1,3,6). It has been suggested that the conserved Ser343 residue in the activation loop plays a key role in the activation of ILK1 (2).
|Human, Monkey, Mouse, Pig, Rat|
Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting
Background: The serum response factor (SRF) is a 67 kDa phospho-protein that, together with auxiliary factors, modulates transcription of immediate early genes containing serum response elements at their promoters (1,2). SRF contains several phosphorylation sites (3), but functional consequences of phosphorylation have not been identified unequivocally. Several growth factor- and calcium-regulated kinases, such as p90RSK and CaM kinase IV, can phosphorylate SRF at Ser103 (4,5), and Ser103 of SRF is also a nuclear target for MAPKAP kinase 2 (6).