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This rabbit anti-IR/IGF1R [pYpYpY1158/1162/1163] polyclonal antibody is specific to human, mouse IR⁄IGF1R [pY1158⁄pY1162⁄pY1163] and expected to react with rat (not tested). IR/IGF1R [pYpYpY1158/1162/1163] polyclonal antibody recognizes the expressed product of the NCL gene. IR and IGF1R are heterotetrameric proteins consisting of two ligand binding α subunits and two β subunits that each contain a tyrosine kinase domain. Validated application for IR/IGF1R [pYpYpY1158/1162/1163] polyclonal antibody is Western blotting.
Applications: validated for Western blotting Host species and isotype: rabbit IgG Reactivity: human, mouse IR⁄IGF1R [pY1158⁄pY1162⁄pY1163]. [Rat (100% homologous) IR/IGF1R has not been tested.] Product size: 10 blots pack size
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 (~95 kDa) are heterotetrameric proteins consisting of two ligandbinding α subunits and two β 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. It is generally believed that autophosphorylation within the activation loop proceeds in a processive manner initiating at the second tyrosine (1162 for the IR or 1135 for the IGF1R), 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.
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