PDGF Receptor α Antibody

3164:

Flow , IHC / Paraffin , Immunoprecipitation , Western Blotting

PDGF Receptor α Antibody detects endogenous levels of PDGF receptor α. This antibody may cross-react with PDGF receptor β.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy-terminal sequence of human PDGF receptor α. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from L6, NIH/3T3 and C2C12 cells, using PDGF Receptor α Antibody.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human gastrointestinal stromal tumor (GIST), using PDGF Receptor α Antibody.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human sarcomatoid neoplasm of the lung, using PDGF Receptor α Antibody.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human synovial sarcoma, using PDGF Receptor α Antibody.

Flow Cytometry

Flow cytometric analysis of NIH/3T3 cells, untreated (blue) or PDGF-treated (green), using PDGF Receptor α Antibody compared to a nonspecific negative control antibody (red).

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). 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).

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.

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

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For Research Use Only. Not For Use In Diagnostic Procedures.