Rat Anti-PDGFRA Recombinant Antibody (2Q1724) (CBMAB-C5342-LY)

Platelet Derived Growth Factor Receptor Alpha

This gene encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. Studies suggest that this gene plays a role in organ development, wound healing, and tumor progression. Mutations in this gene have been associated with idiopathic hypereosinophilic syndrome, somatic and familial gastrointestinal stromal tumors, and a variety of other cancers. [provided by RefSeq, Mar 2012]

Platelet Derived Growth Factor Receptor Alpha; Platelet-Derived Growth Factor Receptor, Alpha Polypeptide; Alpha-Type Platelet-Derived Growth Factor Receptor; Platelet-Derived Growth Factor Receptor 2; CD140 Antigen-Like Family Member A; CD140a Antigen; PDGF-R-Alpha; EC 2.7.10.1; PDGFR-2;

Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca2+ and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. 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.

Adrenal gland developmentIEA:Ensembl
Cardiac myofibril assemblyISS:UniProtKB
Cell activationManual Assertion Based On ExperimentTAS:BHF-UCL
Cell chemotaxisManual Assertion Based On ExperimentIMP:UniProtKB
Cellular response to amino acid stimulusIEA:Ensembl
Cellular response to reactive oxygen speciesManual Assertion Based On ExperimentIDA:MGI
Embryonic cranial skeleton morphogenesisISS:UniProtKB
Embryonic digestive tract morphogenesisISS:UniProtKB
Embryonic skeletal system morphogenesisISS:UniProtKB
Estrogen metabolic processIEA:Ensembl
Extracellular matrix organizationIEA:Ensembl
Face morphogenesisIEA:Ensembl
Hematopoietic progenitor cell differentiationIEA:Ensembl
In utero embryonic developmentIEA:Ensembl
Leydig cell differentiationIEA:Ensembl
Lung developmentIEA:Ensembl
LuteinizationISS:UniProtKB
Male genitalia developmentIEA:Ensembl
Metanephric glomerular capillary formationISS:UniProtKB
Negative regulation of platelet activationManual Assertion Based On ExperimentIDA:UniProtKB
Odontogenesis of dentin-containing toothIEA:Ensembl
Peptidyl-tyrosine phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Phosphatidylinositol-mediated signalingManual Assertion Based On ExperimentIMP:UniProtKB
Platelet aggregationManual Assertion Based On ExperimentIMP:UniProtKB
Platelet-derived growth factor receptor signaling pathwayManual Assertion Based On ExperimentIDA:BHF-UCL
Platelet-derived growth factor receptor-alpha signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of cell migrationManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cell population proliferationManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathwayManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cytosolic calcium ion concentrationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of ERK1 and ERK2 cascadeManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of fibroblast proliferationManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of kinase activityManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of phosphatidylinositol 3-kinase activityManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signalingManual Assertion Based On ExperimentTAS:UniProtKB
Positive regulation of phospholipase C activityManual Assertion Based On ExperimentIMP:UniProtKB
Protein autophosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of actin cytoskeleton reorganizationManual Assertion Based On ExperimentTAS:UniProtKB
Regulation of chemotaxisManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of mesenchymal stem cell differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Retina vasculature development in camera-type eyeISS:UniProtKB
Roof of mouth developmentIEA:Ensembl
Signal transduction involved in regulation of gene expressionIEA:Ensembl
Transmembrane receptor protein tyrosine kinase signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
White fat cell differentiationIEA:Ensembl
Wound healingISS:UniProtKB

Cell membrane
Cell projection, cilium
Golgi apparatus

Gastrointestinal stromal tumor (GIST):
Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery.
GIST-plus syndrome (GISTPS):
A disorder characterized by multiple mesenchymal tumors of the gastrointestinal tract, including gastrointestinal stromal tumor, inflammatory fibroid polyps, and fibroid tumors. Additional features are coarse facies and skin, broad hands and feet, and premature tooth loss. GISTPS is an autosomal dominant disease with incomplete penetrance. Gastrointestinal stromal tumor and inflammatory fibroid polyps may also occur in isolation.

Extracellular: 24-528
Helical: 529-549
Cytoplasmic: 550-1089

N-glycosylated.
Ubiquitinated, leading to its internalization and degradation.
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1.