Human PDGF R alpha Alexa Fluor® 488-conjugated Antibody Summary
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of PDGF R alpha in U‑118‑MG Human Cell Line by Flow Cytometry. U-118-MG human glioblastoma/astrocytoma cell line was stained with Mouse Anti-Human PDGF R alpha Alexa Fluor® 488-conjugated Monoclonal Antibody (Catalog # FAB1264G, filled histogram) or isotype control antibody (Catalog # IC002G, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: PDGF R alpha
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).
- Heldin, C.H. and L. Claesson-Welsh (1994) Guidebook to Cytokines and Their Receptors, Nicola, N.A. (ed) Oxford University Press, New York, NY p. 202.
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