Platelet-derived growth factor receptors exhibit tyrosine-protein kinase activity and have been implicated in the control of cell proliferation, survival and migration. PDGF receptors, PDGFR-alpha and PDGFR-beta, have 5 extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo-and heterodimers. Dimerization of the receptors results in phosphorylation in the complex. More than 10 different SH2-domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF-alpha and beta receptors. PDGF alpha receptors are expressed in oligodendrocyte progenitor cells and PDGF beta receptors are expressed on neurons.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
PDGFR-beta (K745) polyclonal antibody detects endogenous levels of PDGFR-beta protein.
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