The Insulin-like Growth Factor 1 Receptor (IGF1) is also known as CD221, JTK13. and is a transmembrane receptor that is activated by IGF-1 and by the related growth factor IGF-2. It belongs to the large class of tyrosine kinase receptors. This receptor mediates the effects of IGF-1, which is a polypeptide protein hormone similar in molecular structure to insulin. IGF1R is make up of two alpha subunits and two beta subunits, the Both the alpha and beta subunits are synthesized from a single mR precursor. The precursor is then glycosylated, proteolytically cleaved, and crosslinked by cysteine bonds to form a functional transmembrane alphabeta chain.The alpha chains are located extracellularly while the beta subunit spans the membrane and are responsible for intracellular signal transduction upon ligand stimulation. IGF1R have a binding site for ATP, which is used to provide the phosphates for autophosphorylation. There is a 60% homology between IGF1R and the insulin receptor. In response to ligand binding, the alpha chains induce the tyrosine autophosphorylation of the beta chains. This event triggers a cascade of intracellular signaling that, while somewhat cell type specific, often promotes cell survival and cell proliferation.
Application Notes: This protein carries a human IgG1 Fc tag at the C-terminus. The protein has a calculated MW of 129.3 kDa. The protein migrates as 70-75 kDa and 105-115 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation
Immobilized Human IGF-I R, Fc Tag (Cat. No. orb1496214) at 5 µg/mL (100 µL/well) can bind Biotinylated Human IGF-I, Avitag, Fc Tag with a linear range of 0.01-0.625 µg/mL (QC tested).
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