Description
Rat IGF-I R/CD221 Recombinant Protein His Tag Lyophilized has been recombinantly produced in HEK293 cells.
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 mRNA 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.
This protein carries a polyhistidine Tag at the C-terminal. This protein contains a furin convertase cleavage site, 738-RRRR-741, and will be partially processed into N (alpha chain) and C-terminal fragment (partial beta chain) with calculated MW of 81.3 kDa and 24.2 kDa respectively. The protein migrates as 45-50 kDa (partial beta chain), 96-115 kDa (alpha chain) and 120 kDa (alpha chain & partial beta chain) under reducing (R) condition (SDS-PAGE) due to glycosylation