Phospho-PDGFR α/β (Tyr849/Tyr857) Antibody (Rabbit mAb) [B8C12]

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IP1:50

Application
WB, IP

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
123 kDa

Datasheet & SDS

Biological Description

Specificity
Phospho-PDGFR α/β (Tyr849/Tyr857) Antibody (Rabbit mAb) [B8C12] detects endogenous levels of PDGFR α and β only when phosphorylated on Tyr849 of PDGFRα and Tyr857 of PDGFRβ.

Clone
B8C12

Synonym(s)
Activated tyrosine kinase PDGFRB; CD140; CD140A; CD140a antigen; CD140B; IBGC4; IMF1; JTK12; KOGS; PDGF-R-alpha; PDGF-R-beta; PDGFR; PDGFR alpha; PDGFR beta; PDGFR-1; PDGFR-2; PDGFR-alpha; PDGFR-beta; PDGFR1; PDGFR2; PDGFRA; PDGFRalpha

Background
Phosphorylated PDGF receptor α at Tyr849 and PDGF receptor β at Tyr857 represent activation loop phosphotyrosine states of closely related class III receptor tyrosine kinases that define their catalytically active conformation and initiate a network of downstream signaling cascades in response to binding of disulfide‑linked PDGF dimers, including PDGF‑AA, AB, BB, CC and DD, with isoform‑ and dimer‑specific patterns of receptor homodimer and α/β heterodimer engagement. The receptors share a common structural organization composed of an extracellular ligand‑binding region with five immunoglobulin‑like domains, a single transmembrane segment and a cytoplasmic portion containing a split tyrosine kinase domain with an activation loop and a kinase insert, flanked by regulatory sequences in the juxtamembrane and C‑terminal tail; ligand binding drives receptor dimerization and trans‑autophosphorylation, and structural/functional analyses identify Tyr849 in PDGFRα and Tyr857 in PDGFRβ within the activation loop as key autophosphorylation sites whose modification stabilizes the active kinase conformation and is necessary for efficient phosphorylation of additional regulatory tyrosines that serve as docking sites for SH2‑domain signaling effectors. Once Tyr849/Tyr857 are phosphorylated, PDGFRα/β recruit a spectrum of SH2‑containing proteins, including GRB2–SOS to activate RAS–RAF–MEK–ERK, PI3K (via p85 binding to Tyr751 and neighboring sites in PDGFRβ) to stimulate AKT and mTOR signaling, PLCγ to drive DAG/IP₃‑mediated calcium mobilization and PKC activation, SRC family kinases, SHP2 phosphatase and STAT transcription factors, collectively controlling mitogenesis, survival, actin cytoskeleton remodeling, chemotaxis, angiogenesis and differentiation of mesenchymal lineages such as fibroblasts, vascular smooth muscle cells, pericytes and oligodendrocyte precursors. PDGFRα homodimers preferentially bind PDGF‑AA, AB, BB and CC, PDGFRβ homodimers bind PDGF‑BB and PDGF‑DD as well as PDGF‑AB, and α/β heterodimers respond to PDGF‑B, C and D and PDGF‑AB, and these distinct receptor/ligand combinations, together with cell‑type‑specific expression of PDGFRα versus PDGFRβ, define the balance between proliferative and chemotactic responses; PDGFRβ homodimers and α/β heterodimers are strong stimulators of chemotaxis in fibroblasts and smooth muscle cells, whereas PDGFRα homodimers can inhibit chemotaxis and bias signaling toward proliferation, with Tyr849/Tyr857 phosphorylation acting as the primary switch between inactive and signaling‑competent states in each dimer context. PDGF signaling and PDGFRα/β activation loop phosphorylation are central to organ development, including glomerular capillary tuft formation, lung and intestinal epithelial folding and neural crest–derived connective tissue patterning, and aberrations in the PDGF/PDGFR pathway, such as gain‑of‑function receptor mutations or overexpression, lead to uncontrolled mesenchymal proliferation and enhanced angiogenesis characteristic of malignancies, vascular proliferative disorders and fibrotic diseases. Phospho‑specific antibodies recognizing PDGFRα Tyr849 and PDGFRβ Tyr857 are widely used to quantify receptor activation state and PDGF pathway engagement in biochemical assays and tumor samples, and Tyr849/Tyr857 phosphorylation serves as a mechanistic readout in studies of PDGFR inhibitors and modulators of receptor function, which target this activation loop–dependent catalytic activity to block PDGF‑driven growth, migration and neovascularization.

Background

Phosphorylated PDGF receptor α at Tyr849 and PDGF receptor β at Tyr857 represent activation loop phosphotyrosine states of closely related class III receptor tyrosine kinases that define their catalytically active conformation and initiate a network of downstream signaling cascades in response to binding of disulfide‑linked PDGF dimers, including PDGF‑AA, AB, BB, CC and DD, with isoform‑ and dimer‑specific patterns of receptor homodimer and α/β heterodimer engagement. The receptors share a common structural organization composed of an extracellular ligand‑binding region with five immunoglobulin‑like domains, a single transmembrane segment and a cytoplasmic portion containing a split tyrosine kinase domain with an activation loop and a kinase insert, flanked by regulatory sequences in the juxtamembrane and C‑terminal tail; ligand binding drives receptor dimerization and trans‑autophosphorylation, and structural/functional analyses identify Tyr849 in PDGFRα and Tyr857 in PDGFRβ within the activation loop as key autophosphorylation sites whose modification stabilizes the active kinase conformation and is necessary for efficient phosphorylation of additional regulatory tyrosines that serve as docking sites for SH2‑domain signaling effectors. Once Tyr849/Tyr857 are phosphorylated, PDGFRα/β recruit a spectrum of SH2‑containing proteins, including GRB2–SOS to activate RAS–RAF–MEK–ERK, PI3K (via p85 binding to Tyr751 and neighboring sites in PDGFRβ) to stimulate AKT and mTOR signaling, PLCγ to drive DAG/IP₃‑mediated calcium mobilization and PKC activation, SRC family kinases, SHP2 phosphatase and STAT transcription factors, collectively controlling mitogenesis, survival, actin cytoskeleton remodeling, chemotaxis, angiogenesis and differentiation of mesenchymal lineages such as fibroblasts, vascular smooth muscle cells, pericytes and oligodendrocyte precursors. PDGFRα homodimers preferentially bind PDGF‑AA, AB, BB and CC, PDGFRβ homodimers bind PDGF‑BB and PDGF‑DD as well as PDGF‑AB, and α/β heterodimers respond to PDGF‑B, C and D and PDGF‑AB, and these distinct receptor/ligand combinations, together with cell‑type‑specific expression of PDGFRα versus PDGFRβ, define the balance between proliferative and chemotactic responses; PDGFRβ homodimers and α/β heterodimers are strong stimulators of chemotaxis in fibroblasts and smooth muscle cells, whereas PDGFRα homodimers can inhibit chemotaxis and bias signaling toward proliferation, with Tyr849/Tyr857 phosphorylation acting as the primary switch between inactive and signaling‑competent states in each dimer context. PDGF signaling and PDGFRα/β activation loop phosphorylation are central to organ development, including glomerular capillary tuft formation, lung and intestinal epithelial folding and neural crest–derived connective tissue patterning, and aberrations in the PDGF/PDGFR pathway, such as gain‑of‑function receptor mutations or overexpression, lead to uncontrolled mesenchymal proliferation and enhanced angiogenesis characteristic of malignancies, vascular proliferative disorders and fibrotic diseases. Phospho‑specific antibodies recognizing PDGFRα Tyr849 and PDGFRβ Tyr857 are widely used to quantify receptor activation state and PDGF pathway engagement in biochemical assays and tumor samples, and Tyr849/Tyr857 phosphorylation serves as a mechanistic readout in studies of PDGFR inhibitors and modulators of receptor function, which target this activation loop–dependent catalytic activity to block PDGF‑driven growth, migration and neovascularization.

References
https://pubmed.ncbi.nlm.nih.gov/23137658/ https://pubmed.ncbi.nlm.nih.gov/23137658/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%