Overview
- Peptide (C)RQEYRKYGGAKLNR, corresponding to amino acid residues 883-896 of rat IGF1R (Accession P24062). Extracellular, N-terminus (β chain).
- Mouse and rat brain lysates; human MCF-7 breast adenocarcinoma, U-87 MG glioblastoma, and THP-1 monocytic leukemia cell lysates (1:400-1:2000).
Western blot analysis of mouse brain lysate (lanes 1 and 3) and rat brain lysate (lanes 2 and 4):1, 2. Anti-IGF1R (extracellular) Antibody (#ANT-045), (1:400).
3, 4. Anti-IGF1R (extracellular) Antibody, preincubated with IGF1R (extracellular) Blocking Peptide (#BLP-NT045).
- Rat brain sections (1:1200).
- Human THP-1 monocytic leukemia cells (2.5 µg).
Insulin-like growth factor receptor (IGF1R) is a cell surface, tyrosine kinase receptor that can be activated by IGF1, IGF2, and insulin1.
IGF receptors are tyrosine kinase-containing heterotetramers that are linked to numerous cytoplasmic signaling cascades and have important roles in various cellular functions. IGF1R displays potent anti-apoptotic, pro-survival capacities and plays a key role in malignant transformation by regulating MAPK and PI3K/AKT signaling pathways. IGF1R regulators are identified as a candidate therapeutic targets in cancer and growth-related diseases1,2.
IGF1R and insulin receptor (IR) are closely related, and share 57% sequence identity and high structural similarity. Each IGF1R and IR receptor consists of the L1, CR, L2, FnIII-1,-2,-3, transmembrane (TM), and kinase domain. Two such protomers are linked by multiple disulfide bonds, forming a stable, covalent dimer. Upon ligand binding, the dimer undergoes significant conformational changes which facilitate its further signal transduction cascade3.
