Phospho-PDGF Receptor β (Tyr740) (32A9) Rabbit mAb specifically binds to tyrosine phosphorylated PDGF receptor-β, but not other phosphorylated tyrosine kinases. Western blot analysis of extracts from cells expressing different activated tyrosine kinase proteins, using Phospho-PDGF Receptor beta (Tyr740) (32A9) Rabbit mAb (upper) or Phospho-Tyrosine Mouse mAb (P-Tyr-100) #9411 (lower).
Western blot analysis of extracts of NIH/3T3 cells, untreated or stimulated with Platelet-Derived Growth Factor (PDGF) #9909, using Phospho-PDGF Receptor-β (Tyr751) (C63G6) Rabbit mAb (upper) or PDGF Receptor-β (2B3) Mouse mAb #3175 (lower).
Western blot analysis of extracts from NIH/3T3 cells untreated or treated with PDGF-BB, using Phospho-PDGF Receptor beta (Tyr771) (76D6) Rabbit mAb (upper) or PDGF Receptor beta (28E1) Rabbit mAb #3169.
Western blot analysis of cell extracts from NIH/3T3 cells unstimulated or stimulated with PDGF-BB (100 ng/ml for 5 min), using Phospho-PDGF Receptor-β (Tyr1009) (42F9) Rabbit mAb (upper) or PDGF receptor-β (2B3) Mouse mAb #3175 (lower).
Western blot analysis of extracts of NIH/3T3 cells untreated or treated with PDGF-BB, using Phospho-PDGF Receptor β (Tyr1021) (6F10) Rabbit mAb (upper), or PDGF Receptor β (2B3) Mouse mAb (#3175) (lower).
Confocal immunofluorescent analysis of NIH/3T3 cells, serum-starved (left) or PDGF-treated (right), using PDGF Receptor beta (28E1) Rabbit mAb (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
After the primary antibody is bound to the target protein, a complex with HRP-linked secondary antibody is formed. The LumiGLO® is added and emits light during enzyme catalyzed decomposition.
Immunohistochemical analysis of frozen U-87MG xenograft using PDGF Receptor beta (28E1) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma using PDGF Receptor β (28E1) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human glioblastoma using PDGF Receptor β (28E1) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded U-87MG cells, showing membrane localization, using PDGF Receptor β (28E1) Rabbit mAb.
Western blot analysis of extracts from various cell lines, using PDGF Receptor β (28E1) Rabbit mAb.
|Phospho-PDGF Receptor β (Tyr740) (32A9) Rabbit mAb 3168||20 µl||
|Phospho-PDGF Receptor β (Tyr751) (C63G6) Rabbit mAb 4549||20 µl||
||H M||190||Rabbit IgG|
|Phospho-PDGF Receptor β (Tyr771) (76D6) Rabbit mAb 3173||20 µl||
|Phospho-PDGF Receptor β (Tyr1009) (42F9) Rabbit mAb 3124||20 µl||
|Phospho-PDGF Receptor β (Tyr1021) (6F10) Rabbit mAb 2227||20 µl||
||H M R||190||Rabbit IgG|
|PDGF Receptor β (28E1) Rabbit mAb 3169||20 µl||
||H M R||190||Rabbit IgG|
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
The PDGF Receptor β Antibody Sampler Kit provides a fast and economical means of evaluating levels of PDGF Receptor protein phosphorylated at the specified sites, as well as total PDGF receptor levels. The kit contains enough primary and secondary antibody to perform two Western blot experiments per antibody.
All Phospho-PDGF Receptor β Rabbit mAbs detect PDGF Receptor β when phosphorylated at the specified sites. PDGF Receptor β (28E1) Rabbit mAb detects endogenous levels of total PDGF receptor β protein. Some PDGFR antibodies may cross-react with PDGF receptor α or other receptor tyrosine kinases when highly overexpressed. Please consult individual product web pages for more details.
Monoclonal antibody is produced by immunizing animals with a fusion protein containing a carboxy-terminal fragment of human PDGF receptor β; and by immunizing animals with a synthetic phosphopeptides corresponding to residues surrounding Tyr740, Tyr751, Tyr771, Tyr1009 or Tyr1021 of human PDGF receptor β.
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).
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