Phospho-Insulin Receptor beta (panTyr) Matched Antibody Pair

Insulin receptor (InsR) is a heterodimeric membrane receptor tyrosine kinase. It is composed of an extracellular α-subunit containing the ligand binding domain, a β-subunit containing an extracellular domain, a transmembrane domain, and a cytoplasmic tyrosine kinase domain (1). Binding of insulin to InsR results in receptor autophosphorylation and subsequent tyrosine kinase activation (2). This provides a docking site for various adaptor molecules, including insulin receptor substrate (IRS), Gab, and Shc, phosphorylation of which promotes subsequent activation of multiple downstream signaling pathways, including MAPK, PI3K, and TC10 (3,4). These events lead to increased glucose uptake and metabolism, and can promote cell growth. Loss-of-function mutation or desensitization of the InsR are two major contributors to insulin resistance and Type 2 diabetes (5). 1.Yip, C.C. and Ottensmeyer, P. (2003) J Biol Chem 278, 27329-32. 2.Hubbard, S.R. (2013) Cold Spring Harb Perspect Biol 5, a008946. 3.Saltiel, A.R. and Pessin, J.E. (2002) Trends Cell Biol 12, 65-71. 4.Zick, Y. (2001) Trends Cell Biol 11, 437-41. 5.Boucher, J. et al. (2014) Cold Spring Harb Perspect Biol 6, pii: a009191. doi: 10.1101/cshperspect.a009191.