Detection of IL-5 in Human Peripheral Blood Mononuclear Cells by Flow Cytometry. Resting (panel A) and PMA/ionomycin-activated (panel B) human peripheral blood mononuclear cells were stained with Mouse Anti-Human IL‑5 PE‑conjugated Monoclonal Antibody (Catalog # IC605P) and Mouse Anti-Human CD3 epsilon APC‑conjugated Monoclonal Antibody (Catalog # FAB100A). Quadrant markers were set based on control antibody staining (Catalog # IC002P). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
(IL-5) is a 20-21 kDa secreted glycoprotein that belongs to the alpha -helical group
of cytokines (1-3). Unlike other family members, it is present as a
covalently linked antiparallel dimer (4, 5). The cDNA for human IL-5
encodes a signal peptide and a 115 amino acid (aa) mature protein that contains both N- and O-linked carbohydrate.
Mature human IL-5 shares 70%, 70%, 62%, 71%, 70% and 66%, aa sequence
identity with mouse, rat, canine, equine, feline and porcine IL-5, respectively. IL-5 is
primarily produced by CD4+ Th2 cells, but also by activated
eosinophils, mast cells, EBV-transformed B cells, group 2 ILCs, macrophages, and IL‑2‑stimulated invariant natural killer T
cells (iNKT) (1, 3, 6-9). IL-5 increases production and mobilization
of eosinophils and CD34+ progenitors from the bone marrow and
causes maturation of eosinophil precursors outside the bone marrow
(1, 6, 10). The receptor for human IL-5, mainly expressed by
eosinophils, but also found on basophils and mast cells, consists of a
unique ligand-binding subunit (IL-5 R alpha ) and a shared signal‑transducing
subunit, beta c (3, 6, 11). IL-5 R alpha first binds IL-5 at low affinity, then
associates with preformed beta c dimers, forming a high-affinity receptor
(12). IL-5 also binds proteoglycans, potentially enhancing its activity
(13). Soluble forms of IL-5 R alpha antagonize IL-5 and can be found in vivo
(10, 14). In humans, IL-5 primarily affects cells of the eosinophilic
lineage, and promotes their differentiation, maturation, activation,
migration and survival, while in mice IL-5 also enhances Ig class
switching and release from B1 cells (1 ‑ 3, 9, 10, 15, 16). IL-5 also
promotes differentiation of basophils and primes them for histamine and
leukotriene release (17).
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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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