CD140b (pY857) Mouse, Alexa Fluor 488, Clone: J24-618, 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 dimerization 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, compartments that are enriched in several of its downstream effectors, including phosphatidylinositol 3'-kinase, Src, and phospholipase C-γ
• The J24-618 monoclonal antibody recognizes the phosphorylated tyrosine 857 (pY857) in the tyrosine kinase domain 2 of CD140b, which is required for maximal receptor kinase activity
• The orthologous phosphorylation site in mouse PDGFRβ is Y856.