Recombinant Human IGFBP-3 Protein, CF Summary
Accession # P17936
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Insulin-like growth factor binding protein-3 (IGFBP-3) is one of six members of the insulinlike growth factor (IGF) binding protein superfamily which function to modulate the biological activity of IGF (1). Human 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, human IGFBP-3 includes a cysteine-rich C-terminal domain, a highly variable central linker domain, and another
N-terminal cystein-erich domain (2, 3). Human 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 human IGFBP-3 shares 82% aa sequence identity with both mouse and rat IGFBP-3. Posttranslational 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.
Citation for Recombinant Human IGFBP-3 Protein, CF
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.
1 Citation: Showing 1 - 1
The IGFBP3/TMEM219 pathway regulates beta cell homeostasis
Authors: F D'Addio, A Maestroni, E Assi, M Ben Nasr, G Amabile, V Usuelli, C Loretelli, F Bertuzzi, B Antonioli, F Cardarelli, B El Essawy, A Solini, IC Gerling, C Bianchi, G Becchi, S Mazzucchel, D Corradi, GP Fadini, D Foschi, JF Markmann, E Orsi, J Škrha, MG Camboni, R Abdi, AM James Shap, F Folli, J Ludvigsson, S Del Prato, G Zuccotti, P Fiorina
Nature Communications, 2022;13(1):684.
Sample Types: Whole Tissue
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