|Detection of IGF‑II R in Human Monocytes by Flow Cytometry. Human whole blood monocytes were stained with Goat Anti-Human IGF‑II R Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF2447, filled histogram) or control antibody (Catalog # AB-108-C, open histogram), followed by Phycoerythrin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0107).|
|IGF‑II R in Human Placenta. IGF‑II R was detected in immersion fixed paraffin-embedded sections of human placenta using 10 µg/mL Goat Anti-Human IGF‑II R Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2447) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
The type 2 insulin-like growth factor receptor (also known as cation-independent mannose-6 phosphate receptor/CI-MPR) is a 300 kDa member of the P-type lectin family of molecules. P-type lectins generate functional eukaryotic lysosomes by binding and sorting lysosomal enzymes expressing phosphorylated mannose residues (M6P) (1-3). IGF-II R is a type I transmembrane glycoprotein that contains a 2,264 amino acid (aa) extracellular region, a 23 aa transmembrane segment and a 124 aa cytoplasmic tail (4, 5). The extracellular region consists of 15 contiguous “binding” repeats of about 150 aa each. The odd-numbered repeats interact with “ligands” while the even-numbered repeats likely generate a nondisulfide homodimer in the membrane (1). Repeat #11 binds IGF-II, while repeats 3 and 9 bind mannose-6 phosphate; repeat #13 contains a fibronectin type II motif and assists in IGF-II binding (1, 2). In the extracellular region of IGF-II R expressed by R&D Systems (600 aa’s), human IGF-II R is 85% aa identical to both mouse and bovine IGF-II R. This expressed region includes binding repeats #11, 12, and 13. In addition to IGF-II, CI-MPR/IGF-II R binds non-M6P containing ligands such as retinoic acid, urokinase-type plasminogen-activator receptor and plasminogen, plus M6P‑containing molecules such as lysosomal enzymes, TGF-beta 1 precursor, proliferin, LIF, CD26, herpes simplex glycoprotein D, and granzymes A and B (2, 6). IGF-II R regulates many diverse biological functions that range from intracellular trafficking to the internalization of extracellular factors and modulation of cellular responses. It delivers newly synthesized M6P-tagged lysosomal enzymes from the trans-golgi network to endosomes, and facilitates the clearance of extracellular lysosomal and matrix degrading enzymes by internalization into clathrin-coated vesicles and delivery into endosomes. With respect to IGF-II biology, it would appear that IGF-II R is principally a regulator of local IGF-II levels, targeting IGF-II for destruction in lysosomes (2). However, some evidence suggests the receptor will signal via G‑proteins, an effect that has yet to be conclusively shown (6).
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