CST, 3161S, Phospho-PDGF Receptor beta (Tyr751) Antibody

Polyclonal Antibody for studying PDGFR-b (Tyr751) phosphate. Validated for Western Blotting,Flow Cytometry (Fixed/Permeabilized). Highly specific and rigorously validated in-house, Phospho-PDGF Receptor beta (Tyr751) Antibody (CST #3161) is ready to ship. Product Usage Information Western Blotting: 1:1000 Flow Cytometry (Fixed/Permeabilized): 1:200 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Flow Cytometry (Fixed/Permeabilized) Specificity / Sensitivity Phospho-PDGF Receptor beta (Tyr751) Antibody detects PDGF receptor β only when phosphorylated at Tyr751. This antibody may cross-react with PDGF receptor α when highly overexpressed. Species Reactivity: Human, Mouse, Rat Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr751 of human PDGF receptor β. Antibodies are purified by protein A and peptide affinity chromatography. Background Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8). Alternate Names Activated tyrosine kinase PDGFRB; Beta platelet-derived growth factor receptor; Beta-type platelet-derived growth factor receptor; CD140 antigen-like family member B; CD140B; IBGC4; IMF1; JTK12; KOGS; NDEL1-PDGFRB; PDGF-R-beta; PDGFR; PDGFR beta; PDGFR-1; PDGFR-beta; PDGFR1; PDGFRB; PENTT; PGFRB; platelet derived growth factor receptor beta; Platelet-derived growth factor receptor 1; Platelet-derived growth factor receptor beta; platelet-derived growth factor receptor, beta polypeptide Specification REACTIVITY: H M R SENSITIVITY: Endogenous MW (kDa): 190 SOURCE: Rabbit