|IGFBP‑4 Inhibition of IGF‑II-dependent Cell Proliferation and Neutralization by Human IGFBP‑4 Antibody. Recombinant Human IGFBP‑4 (Catalog # 804-GB) inhibits Recombinant Human IGF-II (Catalog # 292-G2) induced proliferation in the MCF‑7 human breast cancer cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Human IGF-II (14 ng/mL) activity elicited by Recombinant Human IGFBP‑4 (0.3 μg/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IGFBP‑4 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF804). The ND50 is typically 12‑60 µg/mL.|
|IGFBP‑4 in Human Placenta. IGFBP‑4 was detected in immersion fixed paraffin-embedded sections of human placenta (chorionic villi) using 5 µg/mL Goat Anti-Human IGFBP‑4 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF804) overnight at 4 °C. Before incubation with the primary antibody tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained with the Anti-Goat HRP-AEC Cell & Tissue Staining Kit (red; Catalog # CTS009) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
Human IGF binding protein 4 (IGFBP-4) was isolated from human plasma based on its ability to bind immobilized IGF-I. Human IGFBP-4 cDNA encodes a 258 amino acid (aa) residue precursor protein with a predicted 21 aa residue signal peptide that is processed to generate the 237 aa residue mature human IGFBP-4. The human IGFBP-4 contains a potential N-linked glycosylation site and shares approximately 90% amino acid sequence identity with both the mouse and rat IGFBP-4.
According to the nomenclature of IGFBPs defined at the 4th International Symposium of IGFs (1997, Tokyo), six high-affinity IGF binding proteins
(IGFBP-1, -2, -3, ‑4, ‑5, ‑6), and four IGFBP-related proteins (IGFBPr-1, - 2, -3, -4) have been identified. All IGFBPs have a high cysteine content and share conserved cysteine residues that are clustered in the amino- and carboxy-terminal third of the molecule. IGFBPs have been shown to either inhibit or enhance the biological activities of IGF, or act in an IGF-independent manner. Post-translational modification of IGFBPs, including phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins for IGF and may indirectly regulate IGF actions.
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