Human IGF2R Protein, ECD (Extracellular Domain), Fc-fusion, Recombinant

Description :
The mannose 6-phophate receptors (MPRs) are single-pass type I transmembrane glycoproteins that target the newly synthesized hydrolases from the Golgi complex and the cell surface to lysosomes. There are two different MPRs, one of ~300kDa termed CI-MPR (cation-independent) and a smaller, dimeric receptor of ~46kDa termed CD-MPR (cation-depnendent). Both MPRss are P-type lectins that bind terminal mannose 6-phosphate (M6P) with similar affinity (CI-MPR = 7 μM, CD-MPR = 8 μM) and contain similar cytoplasmic signals for intracellular trafficking. CD-MPR contain a 157 amino-acid M6P-binding-domain in the extracellular/luminal region. CI-MPR was also identified as the cell surface receptor for insulin-like growth factor 2 (IGF2R/CD222). IGF2R consists of 15 repeats homologous to the M6P-binding domain in CD-MPR. Repeats #3 and #9 are responsible for binding to M6P. Repeat #11 binds IGF2 while repeat #13 contains a fibronectin type II motif that assists in IGF2 binding. IGF2R regulates many diverse biological processes such as intracellular trafficking, internalization of extracellular factors and modulation of cellular responses. It binds many non­M6P-containing ligands such as retinoic acid, plasminogen­activator receptor and plasminogen, as well as M6P­ containing molecules, including lysosomal enzymes, TGFβ, proliferin, LIF, CD26, herpes simplex glycoprotein D and granzymes. IGF2R acts as a positive regulator of T-cell coactivation by binding CD26. IGF2R also functions in the activation of TGFβ, and the regulation of IGF2 levels. Many studies also show that IGF2R is associated with the progression of tumorigenesis.