|Detection of Human IGFBP‑4 N-terminal Fragment by Western Blot. Western blot shows recombinant human IGFBP-4 N-terminal fragment (10 ng/lane) and recombinant human IGFBP-4 C‑terminal fragment (10 ng/lane). PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human IGFBP‑4 N-terminal Monoclonal Antibody (Catalog # MAB7110) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for IGFBP‑4 N-terminal fragment at approximately 20 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
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) precursor protein with a predicted 21 aa signal peptide that is processed to generate the 237 aa mature human IGFBP-4. The human IGFBP-4 contains a potential N-linked glycosylation site and shares approximately 90% aa 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. IGFBP-4 can be cleaved at Met156-Lys157.
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