Measured by its ability to inhibit the biological activity of IGF-I or IGF-II on MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED50 for this effect is 0.125‑0.5 µg/mL in the presence of 30 ng/mL Recombinant Mouse IGF-II (Catalog # 792-MG).
Source
Mouse myeloma cell line, NS0-derived mouse IGFBP-3 protein Pro22-Gln291 with substitutions Arg250Gln, Gln259Arg, Ser260Gly, Arg271Pro
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
29.4 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.
SDS-PAGE
40-50 kDa, reducing conditions
Publications
Read Publications using 775-B3 in the following applications:
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.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
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 IGFBP-3 Protein, CF
acid stable subunit of the 140 K IGF complex
binding protein 29
binding protein 53
growth hormone-dependent binding protein
IBP-3
IBP3BP-53
IGF-binding protein 3
IGFBP3
IGFBP-3
insulin-like growth factor binding protein 3
insulin-like growth factor-binding protein 3
Background
Insulin-like growth factor binding protein-3 (IGFBP-3) is one of six members of the insulin-like growth factor (IGF) binding protein superfamily which function to modulate the biological activity of IGF (1). IGFBP-3 is the major binding protein of IGF where it exists in circulation as a ternary complex with the acid-labile subunit (ALS) (2). Like other IGFBP members, IGFBP-3 includes a cysteine-rich c-terminal domain, a highly variable central linker domain, and another N-terminal cysteine-rich domain (2, 3). Mouse IGFBP-3 cDNA encodes a 291 amino acid (aa) precursor protein with a 27 aa signal peptide that is processed to generate the 264 aa mature protein. Mature mouse IGFBP-3 shares 82% and 95% aa sequence identity with human and rat IGFBP-3, respectively. Post-translational glycosylation and phosphorylation of IGFBP-3 modifies the affinities of the binding protein. Proteolysis of IGFBP-3 by tissue plasminogen activator (tPA), a disintegrin and metaloproteases (ADAMs), and prostate specific antigen (PSA) contributes to IGFBP-3 degradation or a reduction in its affinity for IGF (4-6). The majority of soluble IGFBP-3 found in circulation is secreted from hepatic non-parenchymal cells. IGFBP-3 expression can be modulated by p53 as well as by various cytokines and growth factors (7, 8). In addition to its role in stabilizing and transporting circulating IGF, IGFBP-3 has been shown to potentiate EGF-EGFR-mediated cell growth through the activation of sphingosine kinase1 (SPHK1) and sphingosin-1-phosphate (S1P) (9, 10). IGFBP-3 has also been shown to modulate adipogenesis (11). Binding of IGFBP-3 to non-IGF-related ligands has been shown to regulate TGF-beta signaling, DNA damage, apoptosis, autophagy, and gene transcription (12). Interactions with non-IGF-related ligands is thought to contribute, in part, to the dichotomous stimulatory and inhibitory effects of IGFBP-3 on cell growth (2).
Shimasaki, S. and N. Ling (1991) Prog. Growth Factor Res. 3:243.
Baxter, R.C. (2013) J. Cell Commun. Signal 7:179.
Baxter, R.C. (2014) Nat. Rev. Cancer 14:329.
Mochizuki, S. et al. (2004) Biochem. Biophys. Res. Commun. 315:79.
Cohen, P. et al. (1994) J. Endocrinol. 142:407.
Bang, P. (1995) Prog. Growth Factor Res. 6:285.
Perks, C.M. and J.M. Holly (2008) J. Mammary Gland Biol. Neoplasia 13:455.
Chan, K. and E.M. Spencer (1997) Endocrine 7:95.
Guix, M. et al. (2008) J. Clin. Invest. 118:2609.
Martin, J.L. et al. (2009) J. Biol. Chem. 284:25542.
Chan, S.S. et al. (2009) Am. J. Physiol. Endocrinol. Metab. 296:E654.
Martin, J.L. and R.C. Baxter (2011) Growth Factors 29:235.
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