Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - Tyrosine Kinase / Adaptors

PDGF Receptor α (D13C6) XP® Rabbit mAb #5241

Applications Reactivity Sensitivity MW (kDa) Isotype
W IHC-P IF-IC F H Endogenous 190 Rabbit IgG

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

PDGF Receptor α (D13C6) XP® Rabbit mAb detects endogenous levels of PDGF receptor α protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein corresponding to the PDGF receptor α extracellular domain.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using PDGF Receptor α (D13C6) XP® Rabbit mAb (upper), PDGF Receptor β (28E1) Rabbit mAb #3169 (middle), and β-Actin Antibody #4967 (lower).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human astrocytoma using PDGF Receptor α (D13C6) XP® Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded NCI-H1703 (PDGFRα+, left) and HCC827 (PDGFRα-, right) cell pellets using PDGF Receptor α (D13C6) XP® Rabbit mAb.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human leiomyosarcoma using PDGF Receptor α (D13C6) XP® Rabbit mAb.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of A-204 cells using PDGF Receptor α (D13C6) XP® Rabbit mAb (blue) compared to a nonspecific negative control antibody (red).

IF-IC

IF-IC

Confocal immunofluorescent analysis of NCI-H1703 (left), A172 (center) and HCC827 cells (right) using PDGF Receptor α (D13C6) XP® Rabbit mAb (green). Actin filaments were labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).


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).

  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.

Application References

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

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