Recombinant Human IGFBP-3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IGFBP-3 Protein, CF Summary

Additional Information
Sf 9 (baculovirus)-expressed
Details of Functionality
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 0.03-0.15 μg/mL in the presence of 14 ng/mL Recombinant Human IGF‑II (Catalog # 292-G2).
Source
Spodoptera frugiperda, Sf 9 (baculovirus)-derived human IGFBP-3 protein
Gly28-Lys291
Accession # P17936
Accession #
N-terminal Sequence
Gly28
Protein/Peptide Type
Recombinant Proteins
Gene
IGFBP3
Purity
>95%, by SDS-PAGE with silver staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
29 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
34-41 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
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 PBS.
Purity
>95%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human 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 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).
  1. Shimasaki, S. and N. Ling (1991) Prog. Growth Factor Res. 3:243.
  2. Baxter, R.C. (2013) J. Cell Commun. Signal 7:179.
  3. Baxter, R.C. (2014) Nat. Rev. Cancer 14:329.
  4. Mochizuki, S. et al. (2004) Biochem. Biophys. Res. Commun. 315:79.
  5. Cohen, P. et al. (1994) J. Endocrinol. 142:407.
  6. Bang, P. (1995) Prog. Growth Factor Res. 6:285.
  7. Perks, C.M. and J.M. Holly (2008) J. Mammary Gland Biol. Neoplasia 13:455.
  8. Chan, K. and E.M. Spencer (1997) Endocrine 7:95.
  9. Guix, M. et al. (2008) J. Clin. Invest. 118:2609.
  10. Martin, J.L. et al. (2009) J. Biol. Chem. 284:25542.
  11. Chan, S.S. et al. (2009) Am. J. Physiol. Endocrinol. Metab. 296:E654.
  12. Martin, J.L. and R.C. Baxter (2011) Growth Factors 29:235.

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Bioinformatics

Gene Symbol IGFBP3
Uniprot