Human IGFBP‑4 N-terminal Antibody

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.