CD140b (pY1009) Mouse, Alexa Fluor 647, Clone: J25-650, BD

Description

• Platelet-derived growth factor (PDGF) is a potent mitogen for cells of mesenchymal origin and exerts its effects by binding to the PDGF receptor (PDGFR), a transmembrane protein tyrosine kinase
• PDGFR is composed of PDGFRα (CD140a) and/or PDGFRβ (CD140b) polypeptides
• Both PDGF and PDGFR consist of subunits that form homo- or heterodimers with varying specificities: PDGF-AA binds only to αα PDGFR, PDGF-AB binds to both αα and αβ PDGFR, and PDGF-BB binds to all three PDGFRs
• Ligand binding induces dime rization and activation of the receptor
• Upon activation, CD140b is phosphorylated at multiple tyrosine sites and, in turn, an intracellular phosphorylation cascade is initiated
• PDGFR localizes primarily to membrane invaginations termed caveolae, compar tments that are enriched in several of its downstream effectors, including phosphatidylinositol 3'-kinase, Src, and phospholipase C-γ(PLC-γ)
• The J25-602 monoclonal antibody recognizes the phosphorylated tyrosine 1009 (pY1009) in the C-terminal noncataly tic region of CD140b, which interacts primarily with protein tyrosine phosphatase 1D and possibly with PLC-γ
• The orthologous phosphorylation site in mouse PDGFRβ is Y1008.