IGF-1R/3T3 mouse fibroblasts transfected with human type I IGF-receptor cDNA was used as the immunogen for the was used as the immunogen for the IGF1R alpha antibody. The epitope has been localized to the alpha subunit, between amino acids 184 and 283.
This antibody is specific for the human insulin-like growth factor 1 receptor (IGF1R). It recognizes the extracellular portion of the receptor, specifically an epitope in the cysteine rich domain of the alpha subunit, between amino acids 184 and 283. It does not cross-react with rat or mouse IGF1R or human insulin receptors in co-precipitation or immuno-depletion assays. The ability of this antibody to bind human IGF1R has been confirmed in IGF1 binding assays using both IG1FR-overexpressing IGF1R/3T3 cells and soluble receptors (Soos et al, 1992). This antibody efficiently precipitates human IGF1R solubilized from IGF1R/3T3 cells (Soos et al, 1992) and human placental membranes (Bailyes et al, 1997), and has been used in immunoprecipitation analysis of 293 cells transfected with IGF1R or chimeric IGF1R-insulin receptor (IR) constructs (Schumacher et al, 1993). When immobilized, this antibody has been shown to remove essentially all soluble, IGF1R/3T3-derived IGF1R (Soos et al, 1992) and human placental membrane-derived IGF1R (Soos et al, 1993) in immuno-depletion experiments. This antibody strongly inhibits IGF1 binding to its receptor (Soos et al, 1992), and has been shown to suppress IGF1-mediated stimulation of skin fibroblast proliferation (Okubo et al 2003).
