PDGF Receptor β (28E1) Rabbit mAb (Biotinylated)Product information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Tyrosine Kinase / Adaptors
PDGF Receptor β (28E1) Rabbit mAb (Biotinylated) #8044
|8044S||100 µl (10 western blots)||---||In Stock||---|
|8044||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat||Endogenous||190||Rabbit IgG|
Species cross-reactivity is determined by western blot using the unconjugated antibody.
Applications Key: W=Western Blotting
Specificity / Sensitivity
PDGF Receptor β (28E1) Rabbit mAb (Biotinylated) recognizes endogenous levels of PDGF receptor β protein. The antibody may cross-react with PDGF receptor α when highly overexpressed.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a GST fusion protein containing a carboxy-terminal fragment of human PDGF receptor β protein.
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated PDGF Receptor β (28E1) Rabbit mAb #3169.
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).
- Deuel, T.F. et al. (1988) Biofactors 1, 213-217.
- Bergsten, E. et al. (2001) Nat. Cell Biol. 3, 512-516.
- Betsholtz, C. et al. (2001) Bioessays 23, 494-507.
- Coughlin, S.R. et al. (1988) Prog. Clin. Biol. Res. 266, 39-45.
- Ostman, A. and Heldin, C.H. (2001) Adv. Cancer Res. 80, 1-38.
- Panayotou, G. et al. (1992) EMBO J. 11, 4261-4272.
- Ramalingam, K. et al. (1995) Bioorg. Med. Chem. 3, 1263-1272.
- 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!
This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.