Detection of IGF‑II R in Human Blood Monocytes by Flow Cytometry.
Human peripheral blood monocytes were stained with Goat Anti-Human IGF‑II R Fluorescein‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB2447F, filled histogram) or isotype control antibody (Catalog # IC108F, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: IGF-II R
The type 2 Insulin-like Growth Factor Receptor (IGF-II R; 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 amino acids), human IGF-II R is 85% 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).
Ghosh, P. et al. (2003) Nat. Rev. Mol. Cell. Biol. 4:202.
Dahms, N.M. and M.K. Hancock (2002) Biochim. Biophys. Acta. 1572:317.
Zaina, S. and J. Nilsson (2003) Curr. Opin. Lipidol. 14:483.
Morgan, D.O. et al. (1987) Nature 329:301.
Oshima, A. et al. (1988) J. Biol. Chem. 263:2553.
Hawkes, C. and S. Kar (2004) Brain Res. Rev. 44:117.
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