Human IL-5 R alpha /CD125 Antibody
Human IL-5 R alpha /CD125 Antibody Summary
Accession # O08665
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.
Detection of IL-5 R alpha/CD125 in HEK293 Human Cell Line Transfected with Human IL-5 R alpha/CD125 and eGFP by Flow Cytometry HEK293 human embryonic kidney cell line transfected with (A) human IL-5 R alpha/CD125 or (B) irrelevant protein, and eGFP was stained with Mouse Anti-Human IL-5 R alpha/CD125 Monoclonal Antibody (Catalog # MAB2531) followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (F0101B). Quadrant markers were set based on control antibody staining (MAB002). Staining was performed using our Staining Membrane-associated Proteins protocol.
Cell Proliferation Induced by IL‑5 and Neutralization by Human IL‑5 R alpha /CD125 Antibody. Recombinant Human IL-5 (205-IL) stimulates proliferation in the TF-1 human erythroleukemic cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human IL-5 (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human IL-5 Ra/CD125 Monoclonal Antibody (MAB2531). The ND50 is typically 0.05-0.5 µg/mL.
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.
Background: IL-5 R alpha/CD125
Interleukin 5, produced primarily by activated T cells and mast cells, has diverse biological effects on a variety of cell types. Human IL-5 is a potent eosinophil differentiation and activation factor in vivo and in vitro. Additionally, it has also been reported that IL-5 can stimulate the proliferation and/or differentiation of basophils and B cells. The multiple effects of IL-5 are mediated by binding of the cytokine to specific cell surface receptors expressed on target cells. As is the case with many other cytokines, the functional high-affinity receptor for IL-5 is a complex consisting of a ligand binding subunit ( alpha chain) and a second subunit ( beta chain) that can modulate the ligand binding affinity of the receptor complex. In the case of IL-5, the beta subunit is shared with the high affinity receptor complexes for IL-3 and GM-CSF. The beta chain does not bind any of the cytokines in question but is indispensable for the cytokine-mediated signaling. cDNA clones for the alpha chain (IL-5 R alpha ) of both the mouse and human high affinity IL-5 receptor complexes have been isolated. Human and mouse IL-5 R alpha are both members of the hematopoietin receptor superfamily characterized by the presence of the WSXWS, and a four cysteine residue motif in the extracellular domain of the transmembrane protein. In addition to the cDNA clone encoding the full-length transmembrane protein, cDNA clones that arise from alternative splicing and that encode soluble secreted forms of IL-5 R alpha have been isolated from mouse as well as human cells. A naturally-occurring soluble form of the IL-5 R alpha has been detected in biological fluids of autoimmune-prone mice and mice bearing chronic B cell leukemia (BCL1). A recombinant human IL-5 soluble receptor alpha has been shown to bind the human IL-5 dimer in a 1:1 ratio and acts as a human IL-5 antagonist. This molecule inhibits the proliferation of IL-5-dependent cell lines and blocks human umbilical cord blood eosinophil differentiation.
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