In a functional ELISA, 0.5-2.5 µg/mL of this antibody will block 50% of the binding of 50 ng/mL of Recombinant Human IGF-II (Catalog # 292-G2) to immobilized Recombinant Human IGF-II R (Catalog # 2447-GR) coated at 2 µg/mL (100 µL/well). At 20 μg/mL, this antibody will block >90% of the binding.
Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
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.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IGF-II R
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).
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.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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