Anti-IGF1R alpha / Insulin like growth factor 1 receptor alpha, clone 24-60

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. 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). Protein function: Receptor tyrosine kinase which mediates actions of insulin- like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R. [The UniProt Consortium]