Human PDGF-AA Antibody

Catalog # Availability Size / Price Qty
MAB2211
MAB2211-SP
Product Details
Citations (1)
FAQs
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Human PDGF-AA Antibody Summary

Species Reactivity
Human
Specificity
Detects human PDGF-AA in direct ELISAs and Western blots. In direct ELISAs, this antibody shows 25% cross-reactivity with recombinant human (rh) PDGF-AB and no cross-reactivity with rhPDGF-BB, rhPlGF, rhVEGF, rhVEGF-C, rhVEGF-D, rhCTGF, or rhLDGF.
Source
Monoclonal Mouse IgG2B Clone # 114503
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
E. coli-derived recombinant human PDGF-AA
Ser87-Thr211
Accession # P04085
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration
Sample
Western Blot
1 µg/mL
Recombinant Human PDGF‑AA (Catalog # 221-AA)

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.

Preparation and Storage

Reconstitution
Reconstitute at 0.5 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 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.

Background: PDGF-AA

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.

Long Name
Platelet-derived Growth Factor AA
Entrez Gene IDs
5154 (Human); 25266 (Rat)
Alternate Names
PDGF1; PDGF-A; PDGFAA; PDGF-AA

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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

  1. Deletion of the mRNA stability factor ELAVL1 (HuR) in pancreatic cancer cells disrupts the tumor microenvironment integrity
    Authors: Grace A McCarthy, Roberto Di Niro, Jennifer M Finan, Aditi Jain, Yifei Guo, Cory R Wyatt et al.
    NAR Cancer

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