Detects mouse IL-15 R alpha in direct ELISAs and Western blots. In direct ELISAs, approximately 5% cross-reactivity with recombinant human (rh) IL‑15 R alpha is observed and less than 1% cross-reactivity with rhIL-2 R alpha, recombinant mouse (rm) IL-2 R beta, and rmIL-2 R gamma is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant mouse IL-15 R alpha Gly33-Lys205 Accession # Q60819
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of IL‑15 R alpha in EL‑4 Mouse Cell Line by Flow Cytometry.
EL‑4 mouse lymphoblast cell line was stained with Goat Anti-Mouse IL‑15 R alpha PerCP‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB551C, filled histogram) or isotype control antibody (Catalog # IC108C, 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-15 R alpha
IL-15R alpha (also known as CD215) is a unique, 52-55 kDa Sushi
domain-containing protein that is produced by a wide variety of cell
types. Mouse IL-15 R alpha is a type I transmembrane glycoprotein that
contains a 173 amino acid (aa) extracellular region (aa 33-205) coupled to a
short 37 aa cytoplasmic tail. It is
found on a wide variety of cells, including hepatocytes, keratinocytes, B
cells, T cells, intestinal columnar epithelium, macrophages, dendritic cells
and select fibroblasts. IL-15 R alpha binds soluble,
15-19 kDa monomeric IL-15 with high affinity, and effectively and serves as a
heterodimeric partner for the cytokine.
Most (if not all) effects attributable to IL-15 are mediated by the
heterodimeric IL-15:IL-15 R alpha complex that
binds to two signaling subunits, the 72-76 kDa IL-2R beta subunit, and the 64-65 kDa common gamma chain ( gamma c).
The latter two subunits have a
restricted expression pattern and generally relate to hematopoietic cells. The IL-15:IL-15 R alpha complex exists in two forms. The first form finds IL-15 bound to
transmembrane IL-15 R alpha, while the second
form finds IL-15 bound to soluble IL-15 R alpha,
a product of proteolytic cleavage. This
soluble complex may exist as a 140-160 kDa heteromultimer. Functionally, the transmembrane IL-15:IL-15 R alpha complex appears to be the most
important. Typically, IL-15 binds
transmembrane IL-15 R alpha in the ER, and
this complex is then presented on the cell surface where it acts in-trans on adjacent IL-2R beta : gamma c expressing cells. Alternatively, the IL-15:IL-15 R alpha complex may also act in-cis, particularly on hematopoietic (or T) cells. In mouse, in-trans
presentation is considered crucial to IL-15 activity, while the human system
appears to utilize both in-trans and in-cis mechanisms. The function of the soluble complex is
unclear; on the one hand, its creation via proteolytic cleavage is suggested to
act as a neutralizer of IL-15 activity, while on the other hand, it is proposed
to serve as a cytokine "hormone" that activates NK and CD8+ T cells at distant
sites. Mouse IL-15 R alpha has at least five isoform variants, two of
which are incapable of binding IL-15. The
first isoform shows a Met substitution for aa 1-206. The second isoform utilizes an alternative
start site at Met141, precluding the existence of an IL-15 Sushi binding domain
over aa 34-98. The remaining three
isoforms contain the ligand binding Sushi domain, but exhibit deletions of aa
129-161, aa 129-194, and aa 98-195. On
balance, the IL-15:IL-15 R alpha system is
considered crucial for generating and maintaining central and effector memory
CD8+ T cells, NK cells and NKT cells.
Over aa 33-205, mouse IL-15 R alpha
shares 89% and 59% aa sequence identity with rat and human IL-15 R alpha, respectively.
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