- Diagnostic Products
- Research Products
|Background:||Biological actions of insulin and IGF1 are mediated by their respective cell surface receptors, both of which are receptor tyrosine kinases that regulate multiple signaling pathways through activation of a series of phosphorylation cascades. The IR and IGF1R are heterotetrameric proteins consisting of two ligand-binding subunits and two subunits that each contain a tyrosine kinase domain. Insulin/IGF1 binding to the extracellular domain leads to autophosphorylation of the receptor and activation of the intrinsic tyrosine kinase activity, which allows appropriate substrates to be phosphorylated. These two receptors differ in sequence in regions that confer specificity for the designated ligand as well as in certain intracellular signaling domains. These differences allow insulin and IGF-1 to regulate different physiological functions through receptors that share a very similar structure. Phosphorylation sites that are unique to each receptor presumably play a key role in these signaling differences. The catalytic loops within the tyrosine kinase domains of the IR/IGF1R contain a three tyrosine motif corresponding to Tyr1158, 1162 and 1163 (for the IR) and Tyr1131, 1135 and 1136 (for the IGF1R). It is generally believed that autophosphorylation within the activation loop proceeds in a processive manner initiating at the second tyrosine (1162 or 1135), followed by phosphorylation at the first tyrosine (1158 or 1131), then the last (1163 or 1136), upon which the IR or IGF1R becomes fully active.|
|Regulatory Statement:||For Research Use Only. Not for use in diagnostic procedures.|
|Product Type:||Primary Antibody|
Applications: WB, IH
There are no references for Phospho-IR/IGF1R [Tyr1158] Polyclonal Antibody at this time.