Anti-Human IGF2R Antibody Pair

Product Description: Insulin-like growth factor 2 receptor (IGF2R), also known as the cation-independent mannose-6-phosphate receptor, is a large, multifunctional transmembrane protein ubiquitously expressed in human tissues. Structurally, IGF2R is composed of a 300-kDa polypeptide with a substantial extracellular region containing 15 homologous domains, a single transmembrane segment, and a short cytoplasmic tail. Its primary functions include binding and internalizing insulin-like growth factor 2 (IGF2) to regulate its signaling, as well as trafficking lysosomal enzymes by recognizing mannose-6-phosphate tags and directing these enzymes from the Golgi apparatus to lysosomes. Specific domains within the extracellular region are responsible for binding IGF2 and phosphomannosyl residues, with domain 11 being critical for IGF2 binding and domains 3, 5, and 9 for mannose-6-phosphate recognition. Beyond its physiological roles, IGF2R is implicated in disease, serving as a prognostic marker in several cancers, such as cervical, kidney, and liver carcinomas, and its dysfunction can disrupt growth factor regulation and lysosomal enzyme trafficking. Protein Function: Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes (PubMed:18817523, PubMed:2963003). Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex (PubMed:18817523, PubMed:2963003). The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer (PubMed:18817523). This receptor also binds IGF2 (PubMed:18046459). Acts as a positive regulator of T-cell coactivation by binding DPP4 (PubMed:10900005) [The Uniprot Consortium]