Recombinant Mouse IGF-II/IGF2 Protein, CF Summary
| Details of Functionality |
Measured in a serum-free cell proliferation assay using MCF-7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED 50 for this effect is 2-10 ng/mL. |
| Source |
E. coli-derived mouse IGF-II/IGF2 protein Ala25-Glu91 |
| Accession # |
|
| N-terminal Sequence |
Ala25 |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
Igf2 |
| Purity |
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
7.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| Publications |
Read Publications using 792-MG in the following applications:
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Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
| Buffer |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
| Purity |
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse IGF-II/IGF2 Protein, CF
Background
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 is part of a complex system of growth and metabolic-regulating proteins that is particularly important during development. 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). This may indicate that postnatally, IGF-II has either a limited, or local effect only in rodent. For example, 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). The first three receptors initiate downstream signaling events, the IGF-2R sequesters local IGF-II, and the six IGFBPs regulate IGF-II activity in various tissues.
- 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.
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