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Cell Signaling Phospho-Pdgf Receptor Alpha (Tyr754) (23b2) Rabbit mAb
List Price $169.00 Your Price $169.00
Cell Signaling Phospho-Pdgf Receptor Alpha (Tyr754) (23b2) Rabbit mAb - CSSPQ (Additional S&H or Hazmat Fees May Apply)
NETA PART: CSSPQ-2992T
MFG.PART: 2992T
UNSPSC: 12352203
Manufacturer: Cell Signaling
| Size | 20 µl |
| Reactivity | H M |
| Sensitivity | Endogenous |
| Molecular Weight (kDa) | 190 |
| Source/Isotype | Rabbit |
| Application/Dilution | {Western Blotting: 1:1000, Immunoprecipitation: 1:50} |
| Storage | Supplied in 10 mm sodium HEPES (pH 7.5), 150 mm NaCl, 100 µg/mL BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody. |
| Specificity/Sensitivity | Phospho-PDGF Receptor α (Tyr754) (23B2) Rabbit mAb detects endogenous levels of PDGFRα only when phosphorylated at tyrosine 754. The antibody does not cross-react with activated PDGFRβ. |
| Species Reactivity | Human, Mouse |
| Source/Purification | Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr754 of human PDGFRα. |
| 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).Interestingly, PDGFR-alpha was found to be phosphorylated at an additional tyrosine residue, Tyr754, in a heterodimeric complex as compared to the alpha-alpha homodimer. Phosphorylation of this tyrosine residue permits the binding of a specific signal-transducing protein, and thereby initiates signaling pathway(s) from the beta-alpha heterodimer, which are dinstinct from those initiated via homodimeric receptor complexes (8). |
| SKU | CSSPQ-2992T |
|---|---|
| Supplier Part Number | 2992T |
| UM | EA |
| UNSPSC | 12352203 |
| Manufacturer | Cell Signaling |
| MSDS URL | Click here |
| Temperature | -20C |
| CountryOfOrigin | United States |
| ProductLine | CSSPQ |
| Qty | 1 |
| MinOrderQty | 1 |
| Weight | 7.000000 |
| Lead Time | 5 |
| Hazardous | N |
| Energy Star | No |
| Green | No |
| Controlled | N |