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Spreading of PDGFR-alpha-deficient lung fibroblasts was insensitive to increased rigidity, and their migration was not reduced by Rac1-guanine exchange factor (GEF (show ARHGEF2 ELISA Kits))-inhibition. PDGFR-alpha-expressing fibroblasts migrated toward stiffer regions within two-dimensional substrates by increasing migrational persistence (durotaxis).
Histone H3.3K27M and Trp53 (show TP53 ELISA Kits) loss and PDGFRA overexpression accelerates disease onset and increases tumor invasion.
The diabetes-induced increase in PDGFRalpha+ cells may be mediated by FOXO3 up-regulation via the inhibition of the PI3K/Akt signaling pathway in STZ-induced diabetic mice.
Constitutive activation of PDGFRalpha leads to expansion of cartilage underlying the coronal sutures, which contribute to suture closure through endochondral ossification, in a process regulated in part by PI3K/AKT (show AKT1 ELISA Kits) signaling.
OLIG2 (show OLIG2 ELISA Kits) modulates growth factor signaling in two distinct populations of glioma stem cells, characterized by expression of either the epidermal growth factor receptor (EGFR (show EGFR ELISA Kits)) or platelet-derived growth factor receptor alpha.
Conditional knockout of Pdgfra in Pdgfra-expressing tissues in mouse embryos at different embryonic days (E9.5 and E10.5) resulted in multiple developmental anomalies of the frontonasal region, the cranium and the abdominal wall musculature. Furthermore, the day at which the Pdgfra is deleted influences the repertoire of the anomalies of the conditional knockout embryos.
FOXA3 (show FOXA3 ELISA Kits) is a marker of the Sertoli cell lineage and of the adult Leydig cell population, and is a regulator of Pdgfra transcription in Leydig cells.
PDGFRalpha and PDGFRbeta are coexpressed in the craniofacial mesenchyme of mid-gestation mouse embryos and that ablation of Pdgfrb (show PDGFRB ELISA Kits) in the neural crest lineage results in increased nasal septum width, delayed palatal shelf development, and subepidermal blebbing.
The results from this study indicate that PDGF (show PDGFA ELISA Kits) signaling is required for fiber hypertrophy, extracellular matrix production, and angiogenesis that occur during muscle growth.
transient middle cerebral-arterial occlusion (MCAO) was introduced into the mice with conditional Pdgfrb (show PDGFRB ELISA Kits)-gene inactivation, including N-PRbeta-KO mice where the Pdgfrb (show PDGFRB ELISA Kits)-gene was mostly inactivated in the brain except that in vascular pericytes
In vitro activation of PDGFR-alpha leads to translational activation of LAMB1 (show LAMB1 ELISA Kits), which in turn induces an invasive and metastatic phenotype of hepatocellular carcinoma cells exhibiting K19 (show KRT19 ELISA Kits) expression.
PDGFRalpha levels are regulated by SMARCB1 (show SMARCB1 ELISA Kits) expression, and assessment of clinical specimens documents the expression of both PDGFRalpha and FGFR1 (show FGFR1 ELISA Kits) in rhabdoid tumor patients.
The downregulation of platelet-derived growth factor receptor-alpha expression may play a causative role in imatinib-induced thrombocytopenia, a common side effect, in the subset of chronic myeloid leukemia (show BCL11A ELISA Kits) patients with platelet-derived growth factor receptor-alpha +68 GA ins (show INS ELISA Kits)/del, +68 GA del/del, and -909C/A genotypes.
Data indicate that co-inhibition of FGFR1 (show FGFR1 ELISA Kits) and HER2 (show ERBB2 ELISA Kits) or PDGFRalpha led to enhanced drug responses.
High PDGFRA expression is associated with pathogenesis of malignant peripheral nerve sheath tumor.
The interaction between CSR1 (show SCARA3 ELISA Kits) and SF3A3 (show SF3A3 ELISA Kits) led to migration of SF3A3 (show SF3A3 ELISA Kits) from nucleus to cytoplasm. The cytoplasmic redistribution of SF3A3 (show SF3A3 ELISA Kits) significantly reduced the splicing efficiency of epidermal growth factor receptor (show EGFR ELISA Kits) and platelet-derived growth factor receptor (show PDGFRL ELISA Kits).
PDGFRa amplification in multiple skin lesions of undifferentiated pleomorphic sarcoma
PDGFRA mutations were associated with gastrointestinal stromal tumors.
The PDGFRA kinase domain structure we report in this study has potential to facilitate development of new agents which can inhibit this kinase, including both its activating and drug-resistant mutations.
BRAF (show BRAF ELISA Kits) mutations are rare events in KIT/PDGFRA wild-type gastrointestinal stromal tumors.
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.
platelet-derived growth factor receptor, alpha polypeptide
, alpha-type platelet-derived growth factor receptor-like
, Alpha platelet-derived growth factor receptor precursor (PDGF-R-alpha)
, CD140 antigen-like family member A
, PDGF alpha chain
, alpha-type platelet-derived growth factor receptor
, platelet-derived growth factor alpha receptor
, platelet-derived growth factor receptor alpha
, alpha platelet-derived growth factor receptor
, CD140a antigen
, PDGFRA/BCR fusion
, platelet-derived growth factor receptor 2
, rearranged-in-hypereosinophilia-platelet derived growth factor receptor alpha fusion protein
, tyrosine kinase PDGFR