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Phospho-PDGF Receptor α (Tyr849)/PDGF Receptor β (Tyr857) (C43E9) Rabbit mAb

Phospho-PDGF Receptor α (Tyr849)/PDGF Receptor β (Tyr857) (C43E9) Rabbit mAb #3170

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Supporting Data

REACTIVITY	H M R
SENSITIVITY	Endogenous
MW (kDa)	190
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting
IP-Immunoprecipitation

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat

Product Information

Product Usage Information

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.

For a carrier free (BSA and azide free) version of this product see product #68236.

Protocol

Specificity / Sensitivity

Phospho-PDGF Receptor α (Tyr849)/PDGF Receptor β (Tyr857) (C43E9) Rabbit mAb detects endogenous levels of PDGF receptor α and β only when phosphorylated on Tyr849 of PDGFRα and Tyr857 of PDGFRβ. This antibody may cross-react with other activated tyrosine kinases.

Species Reactivity:

Human, Mouse, Rat

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr857 of human PDGF receptor β.

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).

Database Links

UniProt ID: P16234 , P09619

Entrez-Gene Id: 5156 , 5159

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

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U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.

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