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PDGFRα and Rβ are members of the class III subfamily of receptor tyrosine kinases (RTK) that also includes the receptors for MCSF, SCF, and Flt3 ligand. All class III RTKs are characterized by the presence of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. Ligand-induced receptor dimerization results in autophosphorylation in trans resulting in the activation of several intracellular signaling pathways that can lead to cell proliferation, cell survival, cytoskeletal rearrangement, and cell migration. Many cell types, including fibroblasts and smooth muscle cells, express both the α and β receptors. Others have only the α receptors (oligodendrocyte progenitor cells, mesothelial cells, liver sinusoidal endothelial cells, astrocytes, platelets, and megakaryocytes) or only the β receptors (myoblasts, capillary endothelial cells, pericytes, T cells, myeloid hematopoietic cells, and macrophages). Recombinant mouse and human soluble PDGF Rβ bind PDGF with high affinity and are potent PDGF antagonists.
Western blot: suggested dilution 1:400 - 1:800 IHC-P: suggested dilution 1:50 - 1:100