Human PDGF-AA Antibody
Human PDGF-AA Antibody Summary
Accession # P04085
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Cell Proliferation Induced by PDGF‑AA and Neutralization by Human PDGF‑AA Antibody. Recombinant Human PDGF-AA (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 (25 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human PDGF-AA Polyclonal Antibody (Catalog # AB-221-NA). The ND50 is typically 5-10 µg/mL.
Detection of PDGF‑AA in Breast Cancer. PDGF‑AA was detected in immersion fixed paraffin-embedded sections of Breast Cancer using Goat Anti-Human PDGF‑AA Polyclonal Antibody (Catalog # AB-221-NA) at 15 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in cancer cells. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Platelet-derived growth factor (PDGF) was discovered as a major mitogenic factor present in serum but absent from plasma. It was found to be secreted from the alpha ‑granules of platelets activated during the coagulation of blood to form serum. Subsequent studies have demonstrated that PDGF is not one molecule but three, each a dimeric combination of two distinct but structurally related peptide chains designated A and B. The dimeric isoforms PDGF-AA, AB and BB are differentially expressed in various cell types and their effects are mediated through two distinct receptors, termed alpha and beta. Differences exist in isoform binding to each receptor. In general, PDGF isoforms are potent mitogens for connective tissue cells, including dermal fibroblasts, glial cells, arterial smooth muscle cells and some epithelial and endothelial cells. In addition to its activity as a mitogen, PDGF is chemotactic for fibroblasts, smooth muscle cells, neutrophils and mononuclear cells. Other reported activities for PDGF include stimulation of granule release by neutrophils and monocytes, facilitation of steroid synthesis by Leydig cells, stimulation of neutrophil phagocytosis, inhibition of natural killer (NK) cell activity, stimulation of collagen synthesis, modulation of thrombospondin expression and secretion, stimulation of collagenase activity and secretion, induction of contraction of rat aorta strips in vitro, and transient induction of T cell IL-2 secretion accompanied by a down-regulation of IL-4 and IFN-gamma production, temporary effects that may allow clonal expansion of antigen-activated B and T helper lymphocytes prior to differentiation. PDGF also appears to be ubiquitous in neurons throughout the CNS, where it is suggested to play an important role in neuron survival and regeneration, and in mediation of glial cell proliferation and differentiation.
Citation for Human PDGF-AA Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Fibrocytes boost tumor-supportive phenotypic switches in the lung cancer niche via the endothelin system
Authors: A Weigert, X Zheng, A Nenzel, K Turkowski, S Günther, E Strack, E Sirait-Fis, E Elwakeel, IM Kur, VS Nikam, C Valasaraja, H Winter, A Wissgott, R Voswinkel, F Grimminger, B Brüne, W Seeger, SS Pullamsett, R Savai
Nature Communications, 2022-10-14;13(1):6078.
Sample Types: Whole Cells
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