|Calculated MW||123968 Da|
|Other Names||Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, PDGFR, PDGFR1|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding Tyrosine 857 of human PDGF-Receptor β was used as an immunogen. This antibody detects PDGF-Receptor β phosphorylated at Tyrosine 857. This antibody is predicted to work on human samples, based on sequence analysis only.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PDGF beta Antibody Phospho (pY857) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5- trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation|
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Provided below are standard protocols that you may find useful for product applications.
Human platelet-derived growth factor (PDGF) receptor, is a receptor tyrosine kinase whose activity induces various signalling cascades leading to cell growth and proliferation. Phosphorylation of Tyrosine 857 (pY857) in the catalytic loop of the PDGF Receptor beta has been shown to increase kinase activity. Two major isoforms exist, PDGF receptor-α and PDGF receptor-β. PDGF receptor-β can only bind two specific PDGF isoforms, PDGF-β and PDGF-Δ (1,2). Upon ligand binding, the receptor undergoes autophosphorylation, allowing binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules such as PI kinase (3), Grb2, and Src, among others.
1. Deuel, T.F., et al. Biofactors 1: 213
2. Deuel, T.F., et al. J Clin Invest. 74: 669
3. Kazlauskas, A, et al. Cell 58: 1121
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