Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

Phospho-PDGF Receptor α (Tyr1018) Antibody #4547

Applications Reactivity Sensitivity MW (kDa) Source
W H M Endogenous 190 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-PDGF Receptor α (Tyr1018) Antibody detects PDGFRα only when phosphorylated at Tyr1018. The antibody does not cross-react with activated PDGFRβ. But it may cross-react with other tyrosine phosphorylated protein tyrosine kinases including EGF receptor.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide (KLH-coupled) corresponding to residues surrounding Tyr1018 of human PDGFRα. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of cell extracts from NIH/3T3 cells, untreated or treated with PDGF-AA, using Phospho-PDGF Receptor α (Tyr1018) Antibody (upper) or PDGF Rreceptor α Antibody #3164 (lower).

Background

The proteins of the platelet derived growth factor (PDGF) family 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). PDGF Receptor α homodimers bind all PDGF isoforms except those containing PDGF D. PDGF Receptor β homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGFα/β receptor 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).

Phosphorylation of PDGFRα on Tyr1018 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery. For more information visit www.phosphosite.org, CST's expert curated modfication site knowledge base.

  1. Deuel, T.F. et al. (1988) Biofactors 1, 213-217.
  2. Bergsten, E. et al. (2001) Nat. Cell Biol. 3, 512-516.
  3. Betsholtz, C. et al. (2001) Bioessays 23, 494-507.
  4. Coughlin, S.R. et al. (1988) Prog. Clin. Biol. Res. 266, 39-45.
  5. Ostman, A. and Heldin, C.H. (2001) Adv. Cancer Res. 80, 1-38.
  6. Panayotou, G. et al. (1992) EMBO J. 11, 4261-4272.
  7. Ramalingam, K. et al. (1995) Bioorg. Med. Chem. 3, 1263-1272.
  8. Kashishian, A. et al. (1992) EMBO J. 11, 1373-1382.

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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.

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