Detects human GM-CSF in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant human (rh) G-CSF, rhIL‑1 alpha, rhIL-1 beta, rhIL-2, rhIL-3, rhIL-4, rhIL-6, rhTNF-alpha or rhTNF-beta is observed. Neutralizes the biological activity of both rhGM-CSF and natural human GM-CSF. It will not neutralize the biological activity of recombinant mouse GM-CSF.
Polyclonal Goat IgG
Protein A or G purified
E. coli-derived recombinant human GM-CSF Ala18-Glu144 Accession # P04141
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize GM‑CSF-induced proliferation in the TF‑1 human erythroleukemic cell line. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The Neutralization Dose (ND50) is typically 1-6 µg/mL in the presence of 0.5 ng/mL Recombinant Human GM‑CSF.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Cell Proliferation Induced by GM‑CSF and Neutralization by Human GM‑CSF Antibody.
Recombinant Human GM‑CSF (Catalog # 215-GM) stimulates proliferation in the TF‑1 human erythroleukemic cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human GM‑CSF (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Human GM‑CSF Polyclonal Antibody (Catalog # AB-215-NA). The ND50 is typically 1-6 µg/mL.
Preparation and Storage
Reconstitute at 1 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it 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.
GM-CSF was initially characterized as a factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It is also a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. GM-CSF is produced by a number of different cell types (including T cells, B cells, macrophages, mast cells, endothelial cells, fibroblasts, and adipocytes) in response to cytokine or inflammatory stimuli. On mature hematopoietic cells, GM-CSF is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages, and eosinophils (1, 2). GM-CSF promotes a Th1 biased immune response, angiogenesis, allergic inflammation, and the development of autoimmunity (3‑5). It shows clinical effectiveness in ameliorating chemotherapy-induced neutropenia, and GM-CSF transfected tumor cells are utilized as cancer vaccines (6, 7). The 22 kDa glycosylated GM-CSF, similar to IL-3 and IL-5, is a cytokine with a core of four bundled alpha ‑helices (8‑12). Mature human GM-CSF shares 63%‑70% amino acid sequence identity with canine, feline, porcine, and rat GM-CSF and 54% with mouse GM-CSF. GM-CSF exerts its biological effects through a heterodimeric receptor complex composed of GM-CSF R alpha /CD116 and the signal transducing common beta chain (CD131) which is also a component of the high-affinity receptors for IL-3 and IL-5 (13, 14). In addition, GM-CSF binds a naturally occurring soluble form of GM-CSF R alpha (15). Human GM-CSF is active on canine and feline cells but not on murine cells (16‑18).
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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