|Detection of Human Phospho-PDGF R alpha (Y742) by Western Blot. Western blot shows lysates of human foreskin fibroblast untreated (-) or treated (+) with 100 ng/mL Recombinant Human PDGF-BB (Catalog # 220-BB) for 10 minutes. PVDF membrane was probed with 0.5 µg/mL of Human Phospho-PDGF R alpha (Y742) Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2114), followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for Phospho-PDGF R alpha (Y742) at approximately 190 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PDGF is a major serum mitogen that can exist as a homo- or heterodimeric protein consisting of disulfide-linked PDGF-A and PDGF-B chains. The PDGF-AA, PDGF‑BB and PDGF-AB isoforms have been shown to bind to two distinct cell surface PDGF receptors with different affinities. Whereas PDGF R alpha binds all three PDGF isoforms with high affinity, PDGF R beta binds PDGF-BB and AB, but not PDGF-AA. Both PDGF R alpha and PDGF R beta are members of the class III subfamily of receptor tyrosine kinases (RTK) that also includes the receptors for M-CSF, 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. PDGF binding induces receptor homo-and heterodimerization and signal transduction. The expression of the alpha and beta receptors is independently regulated in various cell types. Only PDGF R alpha is expressed in oligodendrocyte progenitor cells, mesothelial cell and liver endothelial cells. Soluble PDGF-R alpha has been detected in cell conditioned medium and human plasma. Recombinant soluble PDGF R alpha binds PDGF with high affinity and is a potent PDGF antagonist (1).
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