IGF-II (E3F3N) Rabbit mAb #40941
- WB
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 9, 15, 17, 19, 23 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
IGF-II (E3F3N) Rabbit mAb recognizes endogenous levels of total IGF-II protein. This antibody does not cross-react with IGF-I protein. This antibody also cross-reacts with multiple non-specific bands at higher molecular weights with unknown origin.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Cys84 of human IGF-II protein.
Background
Insulin-like growth factor 2 (IGF-II, IGF-2) is a peptide growth factor with structural similarity to insulin and insulin-like growth factor 1 (IGF-I). IGF-II is reported to interact with multiple cell-surface receptors, including type 1 insulin-like growth factor receptor (IGF1R), insulin receptor A isoform (IR-A), and the structurally distinct type-2 IGF receptor (IGF2R) (1,2). Activation of IGF1R and IR-A by IGF-II promotes cell growth, proliferation, apoptosis, and metabolic signaling (3,4); binding of IGF-II to IGF2R (a.k.a. mannose 6-phosphate receptor) results in IGF-II internalization via receptor-mediated endocytosis, and subsequent transport to the lysosome for degradation (5). Serum IGF-II is generally found in complex with insulin-like growth factor binding proteins (IGFBPs), to which it binds with high affinity; this interaction functions to prolong the half-life of IGF-II in circulation (3). IGF-II plays a particularly crucial role in promoting embryonic fetal growth and development (6-9); in rodents, many of these functions are displaced by IGF-I during normal postnatal development, whereas in humans, IGF-II expression is more widely maintained (10). Binding of IGF-II to both IGF1R and IR-A has been shown to promote cancer progression, primarily through promoting cell proliferation and survival (11,12). Small molecules designed to block IGF-II activity are thus being pursued as therapeutic strategies for cancer treatment (13).
- Blyth, A. et al. (2022) Sci Rep 12, 4695.
- Blyth, A.J. et al. (2020) Cells 9, 2276. doi: 10.3390/cells9102276.
- LeRoith, D. et al. (2021) Mol Metab 52, 101245.
- Holly, J.M.P. et al. (2019) Cells 8, 1207. doi: 10.3390/cells8101207.
- Brown, J. et al. (2008) EMBO J 27, 265-76.
- DeChiara, T.M. et al. (1990) Nature 345, 78-80.
- Engström, W. et al. (1998) Cell Prolif 31, 173-89.
- O'Kusky, J. and Ye, P. (2012) Front Neuroendocrinol 33, 230-51.
- Gardner, S. et al. (2011) Mol Endocrinol 25, 128-37.
- LeRoith, D. and Roberts, C.T. (2003) Cancer Lett 195, 127-37.
- Halje, M. et al. (2012) In Vivo 26, 519-26.
- Scalia, P. et al. (2020) Cancers (Basel) 12, 366. doi: 10.3390/cancers12020366.
- Chen, Y.M. et al. (2020) Cells 9, 1098. doi: 10.3390/cells9051098.
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