Mouse IGF-II/IGF2 Biotinylated Antibody Summary
Ala25-Glu91
Accession # P09535
Applications
Mouse IGF-II/IGF2 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 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/IGF2
IGF-II (Insulin-like growth factor II; also multiplication-stimulating polypeptide/MSP and somatomedin-A) is a secreted 8 kDa polypeptide that belongs to the insulin family of peptide growth factors (1, 2, 3). It has been associated with nervous system proliferation and differentiation, myelination, adrenal cortical proliferation, and skeletal growth and differentiation (4). In human, IGF-II is primarily synthesized by the liver, and circulates at high levels in both fetus and adult. In rodent, however, IGF-II levels drop after the perinatal period, an effect attributed to the lack of a key gene promoter (2, 5). Evidence suggests IGF-II may be the intermediary for SHH induction of VEGF attendant with local neovascularization (6). Rodent cells known to express IGF-II include astrocytes (7), hepatocytes (8), osteoblasts (9), embryonic striated muscle cells (10, 11) plus Kupffer cells and Ito cells (12). Mouse IGF-II is synthesized as a 180 amino acid (aa) preproprecursor (13). It contains a 24 aa signal sequence, a 67 aa mature region, and an 89 aa C-terminal prodomain that is alternatively referred to as the E-peptide. Mature IGF-II is 91% and 97% aa identical to human and rat IGF-II, respectively. Proper processing of IGF-II requires the chaperone activity of GRP94 (14). This generates an 8 kDa mature form, an 18 kDa, 156 aa proform, and a potential 11 kDa, 88 aa “Big” form (aa 25-112). This 11 kDa ”Big” form would be equivalent to human 15-16 kDa IGF-II, with the 5 kDa difference attributable to the presence of O-linked glycosylation (15). There is an additional 34 aa proteolytic fragment that is termed preptin and contains aa 93-126 of the preproprecursor. This is distinct from IGF-II, is secreted by pancreatic b‑cells, and facilitates insulin secretion (16, 17). IGF-II has multiple binding partners. It binds to IGF-IR, the Insulin receptor (IR)-type A and IGF-IR:IR-A hybrids, the type 2 IGF receptor (IGF-2R), and IGF binding proteins 1-6 (18, 19).
- LeRoith, D. & C.T. Roberts Jr. (2003) Cancer Lett. 195:127.
- Werner, H. & D. LeRoith (2000) Cell. Mol. Life Sci. 57:932.
- Pavelic, J. et al. (2007) Indian J. Med. Res. 125:511.
- Varela-Nieto, I. et al. (2007) Curr. Pharm. Des. 13:687.
- Rotwein, P. & L.J. Hall (1990) DNA Cell Biol. 10:725.
- Chao, W. & P.A. D-Amore (2008) Cytokine Growth Factor Rev. 19:111.
- Rotwein, P. et al. (1988) Proc. Natl. Acad. Sci. USA 85:265.
- Goya, L. et al. (1999) J. Biol. Chem. 274:24633.
- McCarthy, T.L. et al. (1992) Endocrinology 130:1303.
- Zindy, F. et al. (1992) J. Hepatol. 14:30.
- Holthuizen, P.E. et al. (1993) Regul. Pept. 48:77.
- Merrick, D. et al. (2007) BMC Dev. Biol. 7:65.
- Stempien, M.M. et al. (1986) DNA 5:357.
- Ostrovsky, O. et al. (2009) Mol. Biol. Cell 20:1855.
- Daughaday, W.H. et al. (1993) Proc. Natl. Acad. Sci. USA 90:5823.
- Buchanan, C.M. et al. (2001) Biochem. J. 360:431.
- Cornish, J. et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292:E117.
- Denley, A. et al. (2005) Cytokine Growth Factor Rev. 16:421.
- Belfiore, A. (2007) Curr. Pharm. Des. 13:671.
Product Datasheets
Citations for Mouse IGF-II/IGF2 Biotinylated Antibody
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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Citations: Showing 1 - 3
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Development of a Grp94 inhibitor
Authors: Adam S. Duerfeldt, Laura B. Peterson, Jason C. Maynard, Chun Leung Ng, Davide Eletto, Olga Ostrovsky et al.
Journal of the American Chemical Society
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The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation.
Authors: Ostrovsky O, Ahmed NT, Argon Y
Mol. Biol. Cell, 2009-01-21;20(6):1855-64.
Species: Mouse
Sample Types: Cell Culture Supernates
Applications: ELISA Development -
Clinical pharmacodynamic effects of the growth hormone receptor antagonist pegvisomant: implications for cancer therapy.
Authors: Yin D, Vreeland F, Schaaf LJ, Millham R, Duncan BA, Sharma A
Clin. Cancer Res., 2007-02-01;13(3):1000-9.
Species: Human
Sample Types: Plasma
Applications: ELISA Development
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