Human IGF-1 R (Luc) HEK293 Reporter Cell

• Screen for neutralizing antibodies blocking the stimulation of human IGF-1 protein.

Luc

Frozen in liquid nitrogen

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 α and β subunits are synthesized from a single mRNA precursor. The precursor is then glycosylated, proteolytically cleaved, and crosslinked by cysteine bonds to form a functional transmembrane αβ chain.The α chains are located extracellularly while the β 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 α chains induce the tyrosine autophosphorylation of the β chains. This event triggers a cascade of intracellular signaling that, while somewhat cell type specific, often promotes cell survival and cell proliferation.

IGF-I R