Description
Protocol
Available protocols: ELISA+
Specificity / Sensitivity
The PathScan
Species Reactivity: Human
Background
Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).
Alternate Names
CD221; IGF-I receptor; IGF1R; IGFIR; IGFR; insulin like growth factor 1 receptor; Insulin-like growth factor 1 receptor; Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain; Insulin-like growth factor I receptor; JTK13; MGC142170; MGC142172; MGC18216; soluble IGF1R variant 1; soluble IGF1R variant 2
