Recombinant Human IGFBP-4 Protein, CF

Catalog # Availability Size / Price Qty
804-GB-025
R&D Systems Recombinant Proteins and Enzymes
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Citations (8)
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Recombinant Human IGFBP-4 Protein, CF Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
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 0.03-0.09 µg/mL in the presence of 14 ng/mL recombinant human IGF-II.
Source
Mouse myeloma cell line, NS0-derived human IGFBP-4 protein
Asp22-Glu258, with an N-terminal Met
Accession #
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
26 kDa
SDS-PAGE
32 kDa, reducing conditions

Product Datasheets

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804-GB

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

804-GB

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile 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.
  • 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.
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Background: IGFBP-4

IGFBP-4 (insulin-like growth factor binding protein 4) is member of the IGFBP family of structurally similar secreted glycoproteins that maintain IGF-I and IGF-II in the circulation and direct them to their target tissues (1, 2). Human IGFBP-4 cDNA encodes 258 amino acids (aa) that include a 21 aa signal peptide and a 237 aa cysteine-rich mature protein that contains an N-terminal IGFBP domain, a linker sequence, and a C-terminal thyroglobulin domain. Mature human IGFBP-4 shares 91% aa sequence identity with mouse and rat IGFBP-4, and 97% with canine, bovine, ovine and porcine IGFBP-4. Both domains interact with IGFs, although the N‑terminal domain is primary (2). The linker contains a cleavage site that is accessible by PAPP-A (pregnancy-associated plasma protein A) when IGFs are bound (2, 3). IGFBP-4 fragments detected in the plasma of pregnant women have lowered affinity for IGFs, thus upregulating IGF bioavailability for receptor binding (2). Unlike other family members, IGFBP-4 does not interact with the extracellular matrix or translocate to the nucleus (2). Like other family members, it is expressed early in development and has both IGF-dependent and -independent activities (2, 4). IGFBP-4 expression in mesenchymal stem cells is upregulated by the cardiac transcription factor GATA-4 (5). It then enhances cardiomyocyte differentiation by interacting with Frizzled and LRP proteins, inhibiting canonical Wnt signaling (6, 7). IGF can sequester IGFBP-4 when present, inhibiting its ability to support cardiomyocyte differentiation (3, 4). IGFBP-4 is also upregulated in osteoblasts in response to estrogen (8). Intact or proteolytically cleaved IGFBP-4 may either promote or inhibit cancer cell growth, motility and invasion depending on cell type, tissue and stage of the cancer (9-11). It is shown to inhibit IGF-1- or FGF-2-induced angiogenesis, but not that induced by VEGF (10).

References
  1. Bethel, C.R. et al. (1994) Biochem. Mol. Biol. Int. 34:385.
  2. Forbes, B.E. et al. (2012) Front. Endocrinol. (Lausanne) 3:38.
  3. Gyrup, C. and C. Oxvig  (2007) Biochemistry 46:1972.
  4. Schuller, A.G. et al. (1994) Mol. Cell. Endocrinol. 104:57.
  5. Li, H. et al. (2011) Cytotherapy 13:1057.
  6. Zhu, W. et al. (2008) Nature 454:345.
  7. Minato, A. et al. (2012) Biomaterials 33:515.
  8. Denger, S. et al. (2008) Mol. Endocrinol. 22:361.
  9. Ueno, K. et al. (2011) Int. J. Cancer 129:2360.
  10. Contois, L.W. et al. (2012) J. Biol. Chem. 287:1779.
  11. Moreno, M.J. et al. (2013) Neoplasia 15:554.
Long Name
Insulin-like Growth Factor Binding Protein 4
Entrez Gene IDs
3487 (Human); 16010 (Mouse)
Alternate Names
BP-4; HT29-IGFBP; IBP4insulin-like growth factor-binding protein 4; IGF-binding protein 4; IGFBP4; IGFBP-4; IGFBP-4IBP-4; insulin-like growth factor binding protein 4

Citations for Recombinant Human IGFBP-4 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.

8 Citations: Showing 1 - 8
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  1. Inhibition of longevity regulator PAPP-A modulates tissue homeostasis via restraint of mesenchymal stromal cells
    Authors: M Mohrin, J Liu, J Zavala-Sol, S Bhargava, J Maxwell Tr, A Brito, D Hu, D Brooks, G Koukos, L Alabdulaal, JS Paw, K Hake, G Kolumam, ML Bouxsein, R Baron, Y Kutskova, A Freund
    Aging Cell, 2021;0(0):e13313.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Effects of Transport Duration and Environmental Conditions in Winter or Summer on the Concentrations of Insulin-Like Growth Factors and Insulin-Like Growth Factor-Binding Proteins in the Plasma of Market-Weight Pigs
    Authors: E Wirthgen, S Goumon, M Kunze, C Walz, M Spitschak, A Tuchschere, J Brown, C Höflich, L Faucitano, A Hoeflich
    Front Endocrinol (Lausanne), 2018;9(0):36.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Western Blot
  3. IGFBP-4 and -5 are expressed in first-trimester villi and differentially regulate the migration of HTR-8/SVneo cells.
    Authors: Crosley, Erin J, Dunk, Caroline, Beristain, Alexande, Christians, Julian K
    Reprod Biol Endocrinol, 2015;12(0):123.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Hyperactivation of the insulin-like growth factor receptor I signaling pathway is an essential event for cisplatin resistance of ovarian cancer cells.
    Authors: Eckstein N, Servan K, Hildebrandt B, Politz A, von Jonquieres G, Wolf-Kummeth S, Napierski I, Hamacher A, Kassack MU, Budczies J, Beier M, Dietel M, Royer-Pokora B, Denkert C, Royer HD
    Cancer Res., 2009;69(7):2996-3003.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Mannan-binding lectin-associated serine protease 3 cleaves synthetic peptides and insulin-like growth factor-binding protein 5.
    Authors: Cortesio CL, Jiang W
    Arch. Biochem. Biophys., 2006;449(1):164-70.
    Species: Human
    Sample Types: N/A
    Applications: Enzyme Assay
  6. Insulin-like growth factor-II (IGF-II), IGF-binding protein-3 (IGFBP-3), and IGFBP-4 in follicular fluid are associated with oocyte maturation and embryo development.
    Authors: Wang TH, Chang CL, Wu HM, Chiu YM, Chen CK, Wang HS
    Fertil. Steril., 2006;86(5):1392-401.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Steroids and protein markers in the follicular fluid as indicators of oocyte quality in patients with and without endometriosis.
    Authors: Wunder DM, Mueller MD, Birkhauser MH, Bersinger NA
    J. Assist. Reprod. Genet., 2005;22(6):257-64.
    Species: N/A
    Sample Types: N/A
    Applications: ELISA (Standard)
  8. Matrix metalloproteinase-7 degrades all insulin-like growth factor binding proteins and facilitates insulin-like growth factor bioavailability.
    Authors: Nakamura M, Miyamoto S, Maeda H, Ishii G, Hasebe T, Chiba T, Asaka M, Ochiai A
    Biochem. Biophys. Res. Commun., 2005;333(3):1011-6.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay

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