|Detection of Mouse PDGF R alpha by Western Blot. Western blot shows lysates of mouse uterus tissue and mouse lung tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse PDGF R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1062) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). Specific bands were detected for PDGF R alpha at approximately 160-200 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|PDGF R alpha in Mouse Embryo. PDGF R alpha was detected in immersion fixed frozen sections of mouse embryo using 15 µg/mL Goat Anti-Mouse PDGF R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1062) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific labeling was localized to the plasma membrane of mesenchymal cells. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.|
|PDGF R alpha in Mouse Embryo. PDGF R alpha was detected in immersion fixed frozen sections of mouse embryo using Goat Anti-Mouse PDGF R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1062) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.|
|Cell Proliferation Induced by PDGF‑AA and Neutralization by Mouse PDGF R alpha Antibody. Recombinant Human PDGF‑AA (Catalog # 221-AA) stimulates proliferation in the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human PDGF‑AA (10 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Mouse PDGF R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1062). The ND50 is typically 1-5 µg/mL.|
The platelet-derived growth factor (PDGF) family consists of proteins derived from four genes (PDGF-A, -B, -C, and -D) that form disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and a heterodimer (PDGF-AB) (1, 2). These proteins regulate diverse cellular functions by binding to and inducing the homo- or hetero-dimerization of two receptors (PDGF R alpha and R beta ). Whereas alpha / alpha homo-dimerization is induced by PDGF-AA, -BB, -CC, and -AB, alpha / beta hetero-dimerization is induced by PDGF-AB, -BB, -CC, and -DD, and beta / beta homo-dimerization is induced only by PDGF-BB and -DD (1-4). Both PDGF R alpha and R beta are members of the class III subfamily of receptor tyrosine kinases (RTK) that also includes the receptors for M-CSF, SCF, and Flt-3 ligand. All class III RTKs are characterized by the presence of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. Ligand-induced receptor dimerization results in autophosphorylation in trans resulting in the activation of several intracellular signaling pathways that can lead to cell proliferation, cell survival, cytoskeletal rearrangement, and cell migration. Many cell types, including fibroblasts and smooth muscle cells, express both the alpha and beta receptors. Others have only the alpha receptors (oligodendrocyte progenitor cells, mesothelial cells, liver sinusoidal endothelial cells, astrocytes, platelets, and megakaryocytes) or only the beta receptors (myoblasts, capillary endothelial cells, pericytes, T cells, myeloid hematopoietic cells, and macrophages) (1, 2). Recombinant mouse and human soluble PDGF R beta bind PDGF with high affinity and are potent PDGF antagonists.
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