Detection of IL‑13 R alpha 2 in A375 Human Cell Line by Flow Cytometry. A375 human melanoma cell line was stained with Goat Anti-Human IL‑13 R alpha 2 APC‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB614A, filled histogram) or isotype control antibody (Catalog # IC108A, open histogram). View our protocol for Staining Membrane-associated Proteins.
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.
Background: IL-13 R alpha 2
Interleukin-13 Receptor alpha 2 (IL-13 R alpha 2), also
CD213 alpha 2, is a 55-57 kDa member of the type I cytokine receptor family of
molecules. Human IL-13 R alpha 2 is a 354
amino acid (aa) type I transmembrane glycoprotein that contains a 317 aa
extracellular domain (ECD) characterized by three fibronectin type III domains
(aa 27-343). It is expressed by a
limited number of cell types, principally those associated with the respiratory
system. These cells include fibroblasts,
type II alveolar and visceral smooth muscle cells, pseudostratified ciliated
epithelium, goblet cells and possibly monocytes. Notably, IL-13 R alpha 2 is often found to be
intracellular, rather than plasma membrane expressed, and this may reflect
storage deposits that can be quickly accessed when needed. IL-13 R alpha 2 is one of two IL-13Rs that bind IL-13. The principal, but low affinity receptor for
IL-13 is a 65 kDa transmembrane protein termed IL-13 R alpha 1. Following binding to IL-13, this protein
complexes with an adjacent IL-4 R alpha receptor on the cell surface to form a high
affinity, functional receptor signaling complex for IL-13. Within this system, IL-13 R alpha 2 has been
described as a "decoy receptor" that binds to circulating IL-13, rendering it
unavailable for IL-13 R alpha 1 binding.
Supporting this view is the fact that there does not appear to be any
canonical signaling motif in IL-13 R alpha 2s short cytoplasmic tail, and the fact that
soluble IL-13 R alpha 2
will bind to IL-13 and neutralize its effects on target cells in culture. The latter point is of particular importance
when it is recognized that IL-13 R alpha 2 has a naturally circulating soluble splice
form in mouse. Studies in human,
however, suggest a more complicated situation.
First, it is unclear if human actually has circulating IL-13 R alpha 2. Unlike in mouse, there is no potential alternative
splice form in human that could generate a soluble isoform. And while MMP-8 has been identified as a
potential mediator of IL-13 R alpha 2 proteolytic cleavage, such activity would appear
to generate rather small quantities of soluble IL-13 R alpha 2. As a transmembrane protein, IL-13 R alpha 2 is suggested
to interact with IL-4 R alpha, and this likely will result in a downregulation
of IL-13 activity. Thus, IL-13 R alpha 2, while
not a decoy receptor, could act as a negative modulator of IL-13 signaling. On the other hand, the cytoplasmic tail of
IL-13 R alpha 2
is now believed to stimulate AP-1 activity, and the IL-13:IL-13 R alpha 2
transmembrane complex has been identified as a component of a larger signaling
receptor complex for the GH-18 (Glycosyl Hydrolase 18) family member
YKL40/Chi3L1. As such, IL-13 R alpha 2 is
likely to exhibit multiple actions in a system and species-specific manner. Over aa 27-342, human and mouse IL-13 R alpha 2 share
64% aa sequence identity.
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